Structural basis for substrate recognition mechanism of human SLC26A7

Solute carrier family 26 (SLC26) mainly mediates transmembrane transport of various anion ions, including chloride and other halide ions, bicarbonate, oxalate, and sulfate. Many severe hereditary human diseases are correlated with SLC26 protein mutations. Here we report cryo-EM structures of human S...

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Published inNature communications Vol. 16; no. 1; pp. 7600 - 10
Main Authors Li, Xiaorong, Yang, Xiaoxu, Lu, Xiaoli, Lin, Bingqian, Zhang, Yuanyuan, Huang, Bangdong, Zhou, Yutong, Huang, Jing, Wu, Kun, Zhou, Qiang, Chi, Ximin
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 15.08.2025
Nature Publishing Group
Nature Portfolio
Subjects
101/28
631/45/535/1258
631/45/612
82/80
82/83
9/74
Bicarbonates
Binding Sites
Chloride
Chlorides
Chlorides - metabolism
Congenital diseases
Cryoelectron Microscopy
HEK293 Cells
Humanities and Social Sciences
Humans
Iodides
Iodides - chemistry
Iodides - metabolism
Ions
Kidney stones
Molecular dynamics
Molecular Dynamics Simulation
multidisciplinary
Mutation
Nitrates
Protein Binding
Protein transport
Proteins
Recognition
Science
Science (multidisciplinary)
Substrate Specificity
Sulfate Transporters - chemistry
Sulfate Transporters - genetics
Sulfate Transporters - metabolism
Thyroid gland
Transmembrane proteins
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Abstract Solute carrier family 26 (SLC26) mainly mediates transmembrane transport of various anion ions, including chloride and other halide ions, bicarbonate, oxalate, and sulfate. Many severe hereditary human diseases are correlated with SLC26 protein mutations. Here we report cryo-EM structures of human SLC26A7 in apo and iodide binding states. We identify non-canonical binding site for halide ions in SLC26A7. Molecular dynamics simulation and electrophysiological assay confirm the functional importance of key residues involved in iodide and chloride coordination. Together, our discovery marks a step towards an in-depth understanding of SLC26 family protein transport mechanisms. Solute carrier family 26 (SLC26) mediates transmembrane transport of negatively charged ions. Here, the authors report cryo-EM structures of human SLC26A7 in apo and iodide binding states, providing insight into the ion recognition mechanism of SLC26 family proteins.
AbstractList Solute carrier family 26 (SLC26) mainly mediates transmembrane transport of various anion ions, including chloride and other halide ions, bicarbonate, oxalate, and sulfate. Many severe hereditary human diseases are correlated with SLC26 protein mutations. Here we report cryo-EM structures of human SLC26A7 in apo and iodide binding states. We identify non-canonical binding site for halide ions in SLC26A7. Molecular dynamics simulation and electrophysiological assay confirm the functional importance of key residues involved in iodide and chloride coordination. Together, our discovery marks a step towards an in-depth understanding of SLC26 family protein transport mechanisms.Solute carrier family 26 (SLC26) mediates transmembrane transport of negatively charged ions. Here, the authors report cryo-EM structures of human SLC26A7 in apo and iodide binding states, providing insight into the ion recognition mechanism of SLC26 family proteins.
Solute carrier family 26 (SLC26) mainly mediates transmembrane transport of various anion ions, including chloride and other halide ions, bicarbonate, oxalate, and sulfate. Many severe hereditary human diseases are correlated with SLC26 protein mutations. Here we report cryo-EM structures of human SLC26A7 in apo and iodide binding states. We identify non-canonical binding site for halide ions in SLC26A7. Molecular dynamics simulation and electrophysiological assay confirm the functional importance of key residues involved in iodide and chloride coordination. Together, our discovery marks a step towards an in-depth understanding of SLC26 family protein transport mechanisms.
Abstract Solute carrier family 26 (SLC26) mainly mediates transmembrane transport of various anion ions, including chloride and other halide ions, bicarbonate, oxalate, and sulfate. Many severe hereditary human diseases are correlated with SLC26 protein mutations. Here we report cryo-EM structures of human SLC26A7 in apo and iodide binding states. We identify non-canonical binding site for halide ions in SLC26A7. Molecular dynamics simulation and electrophysiological assay confirm the functional importance of key residues involved in iodide and chloride coordination. Together, our discovery marks a step towards an in-depth understanding of SLC26 family protein transport mechanisms.
Solute carrier family 26 (SLC26) mainly mediates transmembrane transport of various anion ions, including chloride and other halide ions, bicarbonate, oxalate, and sulfate. Many severe hereditary human diseases are correlated with SLC26 protein mutations. Here we report cryo-EM structures of human SLC26A7 in apo and iodide binding states. We identify non-canonical binding site for halide ions in SLC26A7. Molecular dynamics simulation and electrophysiological assay confirm the functional importance of key residues involved in iodide and chloride coordination. Together, our discovery marks a step towards an in-depth understanding of SLC26 family protein transport mechanisms. Solute carrier family 26 (SLC26) mediates transmembrane transport of negatively charged ions. Here, the authors report cryo-EM structures of human SLC26A7 in apo and iodide binding states, providing insight into the ion recognition mechanism of SLC26 family proteins.
Solute carrier family 26 (SLC26) mainly mediates transmembrane transport of various anion ions, including chloride and other halide ions, bicarbonate, oxalate, and sulfate. Many severe hereditary human diseases are correlated with SLC26 protein mutations. Here we report cryo-EM structures of human SLC26A7 in apo and iodide binding states. We identify non-canonical binding site for halide ions in SLC26A7. Molecular dynamics simulation and electrophysiological assay confirm the functional importance of key residues involved in iodide and chloride coordination. Together, our discovery marks a step towards an in-depth understanding of SLC26 family protein transport mechanisms.Solute carrier family 26 (SLC26) mainly mediates transmembrane transport of various anion ions, including chloride and other halide ions, bicarbonate, oxalate, and sulfate. Many severe hereditary human diseases are correlated with SLC26 protein mutations. Here we report cryo-EM structures of human SLC26A7 in apo and iodide binding states. We identify non-canonical binding site for halide ions in SLC26A7. Molecular dynamics simulation and electrophysiological assay confirm the functional importance of key residues involved in iodide and chloride coordination. Together, our discovery marks a step towards an in-depth understanding of SLC26 family protein transport mechanisms.
ArticleNumber 7600
Author Wu, Kun
Li, Xiaorong
Zhang, Yuanyuan
Huang, Bangdong
Zhou, Yutong
Lu, Xiaoli
Huang, Jing
Lin, Bingqian
Zhou, Qiang
Yang, Xiaoxu
Chi, Ximin
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  organization: State Key Laboratory for Cellular Stress Biology, Innovation Centre for Cell Signaling Network, School of Life Sciences, Xiamen University
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Cites_doi 10.1016/j.jmb.2003.07.013
10.1016/j.mam.2012.07.009
10.1113/jphysiol.2008.154468
10.1021/ct100578z
10.1038/nmeth.4193
10.1038/s41467-021-27915-z
10.1371/journal.pone.0000880
10.1063/1.466711
10.1002/jcc.20084
10.1021/jp309150r
10.1038/nsmb.3091
10.1038/s41586-021-04152-4
10.1038/nmeth.2115
10.1038/ncomms13420
10.1107/S0907444910007493
10.1016/S0263-7855(97)00009-X
10.1152/ajpcell.00027.2020
10.1097/01.ASN.0000135060.83250.07
10.1038/s41421-020-00193-7
10.1016/j.jsb.2005.01.002
10.1038/s42003-019-0503-6
10.1152/ajprenal.00219.2003
10.7554/eLife.89635
10.1101/gr.849004
10.1038/ng1297-411
10.1016/j.jsb.2015.11.003
10.1016/j.seppur.2005.12.020
10.1152/physiol.00037.2007
10.1107/S0907444909052925
10.3390/genes12050714
10.1186/s12881-020-01023-z
10.7554/eLife.06980
10.7554/eLife.46986
10.7554/eLife.42166
10.1016/j.ultramic.2013.06.004
10.1371/journal.pone.0097191
10.1038/nmeth.4067
10.1038/ng1196-316
10.7554/eLife.87178
10.1038/s41586-024-07487-w
10.1016/j.cell.2021.07.034
10.1093/hmg/ddg127
10.1038/ncomms5231
10.1371/journal.pcbi.1005659
10.1016/j.cpc.2013.09.018
10.1210/jc.2017-02202
10.3389/fcell.2019.00230
10.1016/j.str.2008.03.005
10.1074/jbc.273.20.12307
10.1152/ajpgi.00454.2002
10.1021/acs.jctc.5b00935
10.1016/j.ajhg.2016.03.026
10.1016/j.bbamem.2020.183238
10.1172/JCI59353
10.1002/pro.3943
10.1113/jphysiol.2008.164863
10.1073/pnas.1209039109
10.1002/wcms.66
10.1074/jbc.M409162200
10.1016/0263-7855(96)00018-5
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References W Humphrey (62792_CR70) 1996; 14
XZ Liu (62792_CR25) 2003; 12
J Li (62792_CR1) 2023; 14
62792_CR39
T Grant (62792_CR47) 2015; 4
XM Chi (62792_CR29) 2023; 42
HY Gee (62792_CR21) 2016; 98
N Yamaguchi (62792_CR19) 2022; 12
62792_CR49
J Huang (62792_CR64) 2017; 14
J Kästner (62792_CR44) 2011; 1
M Zou (62792_CR20) 2018; 103
PB Rosenthal (62792_CR50) 2003; 333
62792_CR41
E Ohana (62792_CR11) 2009; 587
LA Everett (62792_CR23) 1997; 17
J Wang (62792_CR8) 2020; 7
S Petrovic (62792_CR13) 2003; 284
J Ge (62792_CR35) 2021; 184
A Guskov (62792_CR69) 2016; 7
MH Olsson (62792_CR59) 2011; 7
62792_CR4
S Chen (62792_CR52) 2013; 135
P Hoglund (62792_CR6) 1996; 14
D Beglov (62792_CR65) 1994; 100
P Emsley (62792_CR55) 2010; 66
S Barone (62792_CR15) 2004; 15
B Tansel (62792_CR43) 2006; 51
EF Pettersen (62792_CR58) 2021; 30
62792_CR31
S Jo (62792_CR60) 2007; 2
C Butan (62792_CR34) 2022; 13
KH Kim (62792_CR10) 2005; 280
J Ishii (62792_CR5) 2019; 2
K Zhang (62792_CR48) 2016; 193
EF Pettersen (62792_CR57) 2004; 25
A Toure (62792_CR3) 2019; 7
A Ullah (62792_CR14) 2020; 1862
H Satoh (62792_CR22) 1998; 273
W Hu (62792_CR28) 2024; 15
P Eastman (62792_CR62) 2017; 13
SL Alper (62792_CR9) 2013; 34
N Bavi (62792_CR33) 2021; 600
62792_CR27
C Perez (62792_CR68) 2014; 5
J Lee (62792_CR61) 2016; 12
H Futamata (62792_CR36) 2022; 13
X Chi (62792_CR30) 2020; 6
J Lei (62792_CR45) 2005; 150
Q Liu (62792_CR32) 2023; 14
GE Crooks (62792_CR38) 2004; 14
L Wang (62792_CR40) 2024; 15
PD Adams (62792_CR54) 2010; 66
LG Trabuco (62792_CR53) 2008; 16
Y Won (62792_CR66) 2012; 116
KX Kim (62792_CR16) 2014; 9
GA Tribello (62792_CR63) 2014; 185
X Cao (62792_CR17) 2020; 319
ER Geertsma (62792_CR26) 2015; 22
SQ Zheng (62792_CR46) 2017; 14
OS Smart (62792_CR42) 1996; 14
E Lindberg (62792_CR24) 2020; 21
JP Bai (62792_CR37) 2017; 7
62792_CR56
MR Dorwart (62792_CR2) 2008; 23
N Shcheynikov (62792_CR18) 2008; 586
62792_CR51
K Khafizov (62792_CR67) 2012; 109
S Petrovic (62792_CR12) 2004; 286
BY Choi (62792_CR7) 2011; 121
References_xml – volume: 7
  year: 2017
  ident: 62792_CR37
  publication-title: Sci. Rep.
– volume: 333
  start-page: 721
  year: 2003
  ident: 62792_CR50
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2003.07.013
– volume: 34
  start-page: 494
  year: 2013
  ident: 62792_CR9
  publication-title: Mol. Asp. Med.
  doi: 10.1016/j.mam.2012.07.009
– volume: 586
  start-page: 3813
  year: 2008
  ident: 62792_CR18
  publication-title: J. Physiol.
  doi: 10.1113/jphysiol.2008.154468
– volume: 7
  start-page: 525
  year: 2011
  ident: 62792_CR59
  publication-title: J. Chem. Theory Comput.
  doi: 10.1021/ct100578z
– volume: 14
  start-page: 331
  year: 2017
  ident: 62792_CR46
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.4193
– volume: 13
  year: 2022
  ident: 62792_CR34
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-021-27915-z
– volume: 2
  start-page: e880
  year: 2007
  ident: 62792_CR60
  publication-title: Plos ONE
  doi: 10.1371/journal.pone.0000880
– volume: 100
  start-page: 9050
  year: 1994
  ident: 62792_CR65
  publication-title: J. Chem. Phys.
  doi: 10.1063/1.466711
– volume: 14
  year: 2023
  ident: 62792_CR32
  publication-title: Nat. Commun.
– volume: 25
  start-page: 1605
  year: 2004
  ident: 62792_CR57
  publication-title: J. Comput. Chem.
  doi: 10.1002/jcc.20084
– volume: 116
  start-page: 11763
  year: 2012
  ident: 62792_CR66
  publication-title: J. Phys. Chem. A
  doi: 10.1021/jp309150r
– volume: 22
  start-page: 803
  year: 2015
  ident: 62792_CR26
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.3091
– volume: 600
  start-page: 553
  year: 2021
  ident: 62792_CR33
  publication-title: Nature
  doi: 10.1038/s41586-021-04152-4
– ident: 62792_CR51
  doi: 10.1038/nmeth.2115
– volume: 7
  year: 2016
  ident: 62792_CR69
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms13420
– volume: 66
  start-page: 486
  year: 2010
  ident: 62792_CR55
  publication-title: Acta Crystallogr. D. Biol. Crystallogr.
  doi: 10.1107/S0907444910007493
– volume: 14
  start-page: 354
  year: 1996
  ident: 62792_CR42
  publication-title: J. Mol. Graph
  doi: 10.1016/S0263-7855(97)00009-X
– volume: 319
  start-page: C641
  year: 2020
  ident: 62792_CR17
  publication-title: Am. J. Physiol. Cell Physiol.
  doi: 10.1152/ajpcell.00027.2020
– volume: 15
  start-page: 2002
  year: 2004
  ident: 62792_CR15
  publication-title: J. Am. Soc. Nephrol.
  doi: 10.1097/01.ASN.0000135060.83250.07
– volume: 7
  year: 2020
  ident: 62792_CR8
  publication-title: Front. Med.
– volume: 6
  start-page: 55
  year: 2020
  ident: 62792_CR30
  publication-title: Cell Discov.
  doi: 10.1038/s41421-020-00193-7
– volume: 150
  start-page: 69
  year: 2005
  ident: 62792_CR45
  publication-title: J. Struct. Biol.
  doi: 10.1016/j.jsb.2005.01.002
– volume: 2
  start-page: 270
  year: 2019
  ident: 62792_CR5
  publication-title: Commun. Biol.
  doi: 10.1038/s42003-019-0503-6
– volume: 286
  start-page: F161
  year: 2004
  ident: 62792_CR12
  publication-title: Am. J. Physiol. Ren. Physiol.
  doi: 10.1152/ajprenal.00219.2003
– ident: 62792_CR41
  doi: 10.7554/eLife.89635
– volume: 14
  start-page: 1188
  year: 2004
  ident: 62792_CR38
  publication-title: Genome Res
  doi: 10.1101/gr.849004
– volume: 17
  start-page: 411
  year: 1997
  ident: 62792_CR23
  publication-title: Nat. Genet.
  doi: 10.1038/ng1297-411
– volume: 193
  start-page: 1
  year: 2016
  ident: 62792_CR48
  publication-title: J. Struct. Biol.
  doi: 10.1016/j.jsb.2015.11.003
– volume: 51
  start-page: 40
  year: 2006
  ident: 62792_CR43
  publication-title: Sep. Purif. Technol.
  doi: 10.1016/j.seppur.2005.12.020
– volume: 23
  start-page: 104
  year: 2008
  ident: 62792_CR2
  publication-title: Physiology
  doi: 10.1152/physiol.00037.2007
– volume: 66
  start-page: 213
  year: 2010
  ident: 62792_CR54
  publication-title: Acta Crystallogr. D. Biol. Crystallogr.
  doi: 10.1107/S0907444909052925
– ident: 62792_CR4
  doi: 10.3390/genes12050714
– volume: 21
  year: 2020
  ident: 62792_CR24
  publication-title: BMC Med. Genet.
  doi: 10.1186/s12881-020-01023-z
– volume: 4
  year: 2015
  ident: 62792_CR47
  publication-title: Elife
  doi: 10.7554/eLife.06980
– ident: 62792_CR27
  doi: 10.7554/eLife.46986
– ident: 62792_CR49
  doi: 10.7554/eLife.42166
– volume: 135
  start-page: 24
  year: 2013
  ident: 62792_CR52
  publication-title: Ultramicroscopy
  doi: 10.1016/j.ultramic.2013.06.004
– volume: 9
  start-page: e97191
  year: 2014
  ident: 62792_CR16
  publication-title: PLoS ONE
  doi: 10.1371/journal.pone.0097191
– volume: 14
  start-page: 71
  year: 2017
  ident: 62792_CR64
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.4067
– volume: 14
  start-page: 316
  year: 1996
  ident: 62792_CR6
  publication-title: Nat. Genet.
  doi: 10.1038/ng1196-316
– ident: 62792_CR31
  doi: 10.7554/eLife.87178
– volume: 14
  year: 2023
  ident: 62792_CR1
  publication-title: Front. Physiol.
– volume: 15
  year: 2024
  ident: 62792_CR40
  publication-title: Nat. Commun.
– ident: 62792_CR39
  doi: 10.1038/s41586-024-07487-w
– volume: 184
  start-page: 4669
  year: 2021
  ident: 62792_CR35
  publication-title: Cell
  doi: 10.1016/j.cell.2021.07.034
– volume: 12
  start-page: 1155
  year: 2003
  ident: 62792_CR25
  publication-title: Hum. Mol. Genet.
  doi: 10.1093/hmg/ddg127
– volume: 5
  year: 2014
  ident: 62792_CR68
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms5231
– volume: 13
  start-page: e1005659
  year: 2017
  ident: 62792_CR62
  publication-title: PLoS Comput. Biol.
  doi: 10.1371/journal.pcbi.1005659
– volume: 185
  start-page: 604
  year: 2014
  ident: 62792_CR63
  publication-title: Comput Phys. Commun.
  doi: 10.1016/j.cpc.2013.09.018
– volume: 103
  start-page: 1889
  year: 2018
  ident: 62792_CR20
  publication-title: J. Clin. Endocrinol. Metab.
  doi: 10.1210/jc.2017-02202
– ident: 62792_CR56
– volume: 7
  start-page: 230
  year: 2019
  ident: 62792_CR3
  publication-title: Front. Cell Dev. Biol.
  doi: 10.3389/fcell.2019.00230
– volume: 15
  year: 2024
  ident: 62792_CR28
  publication-title: Nat. Commun.
– volume: 16
  start-page: 673
  year: 2008
  ident: 62792_CR53
  publication-title: Structure
  doi: 10.1016/j.str.2008.03.005
– volume: 273
  start-page: 12307
  year: 1998
  ident: 62792_CR22
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.273.20.12307
– volume: 284
  start-page: G1093
  year: 2003
  ident: 62792_CR13
  publication-title: Am. J. Physiol. Gastrointest. Liver Physiol.
  doi: 10.1152/ajpgi.00454.2002
– volume: 12
  start-page: 405
  year: 2016
  ident: 62792_CR61
  publication-title: J. Chem. Theory Comput.
  doi: 10.1021/acs.jctc.5b00935
– volume: 98
  start-page: 1228
  year: 2016
  ident: 62792_CR21
  publication-title: Am. J. Hum. Genet.
  doi: 10.1016/j.ajhg.2016.03.026
– volume: 13
  year: 2022
  ident: 62792_CR36
  publication-title: Nat. Commun.
– volume: 1862
  year: 2020
  ident: 62792_CR14
  publication-title: Biochim. Biophys. Acta Biomembr.
  doi: 10.1016/j.bbamem.2020.183238
– volume: 121
  start-page: 4516
  year: 2011
  ident: 62792_CR7
  publication-title: J. Clin. Investig.
  doi: 10.1172/JCI59353
– volume: 30
  start-page: 70
  year: 2021
  ident: 62792_CR58
  publication-title: Protein Sci.
  doi: 10.1002/pro.3943
– volume: 587
  start-page: 2179
  year: 2009
  ident: 62792_CR11
  publication-title: J. Physiol.
  doi: 10.1113/jphysiol.2008.164863
– volume: 12
  year: 2022
  ident: 62792_CR19
  publication-title: Sci. Rep.
– volume: 42
  start-page: 21
  year: 2023
  ident: 62792_CR29
  publication-title: J. Chin. Electron Microsc.
– volume: 109
  start-page: E3035
  year: 2012
  ident: 62792_CR67
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.1209039109
– volume: 1
  start-page: 932
  year: 2011
  ident: 62792_CR44
  publication-title: Wiley Interdiscip. Rev. Comput. Mol. Sci.
  doi: 10.1002/wcms.66
– volume: 280
  start-page: 6463
  year: 2005
  ident: 62792_CR10
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M409162200
– volume: 14
  start-page: 33-38, 27
  year: 1996
  ident: 62792_CR70
  publication-title: J. Mol. Graph
  doi: 10.1016/0263-7855(96)00018-5
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Snippet Solute carrier family 26 (SLC26) mainly mediates transmembrane transport of various anion ions, including chloride and other halide ions, bicarbonate, oxalate,...
Abstract Solute carrier family 26 (SLC26) mainly mediates transmembrane transport of various anion ions, including chloride and other halide ions, bicarbonate,...
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SubjectTerms 101/28
631/45/535/1258
631/45/612
82/80
82/83
9/74
Bicarbonates
Binding Sites
Chloride
Chlorides
Chlorides - metabolism
Congenital diseases
Cryoelectron Microscopy
HEK293 Cells
Humanities and Social Sciences
Humans
Iodides
Iodides - chemistry
Iodides - metabolism
Ions
Kidney stones
Molecular dynamics
Molecular Dynamics Simulation
multidisciplinary
Mutation
Nitrates
Protein Binding
Protein transport
Proteins
Recognition
Science
Science (multidisciplinary)
Substrate Specificity
Sulfate Transporters - chemistry
Sulfate Transporters - genetics
Sulfate Transporters - metabolism
Thyroid gland
Transmembrane proteins
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Title Structural basis for substrate recognition mechanism of human SLC26A7
URI https://link.springer.com/article/10.1038/s41467-025-62792-w
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Volume 16
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