Structural Basis for Rare Earth Element Recognition by Methylobacterium extorquens Lanmodulin
Lanmodulin (LanM) is a high-affinity lanthanide (Ln)-binding protein recently identified in Methylobacterium extorquens, a bacterium that requires Lns for the function of at least two enzymes. LanM possesses four EF-hands, metal coordination motifs generally associated with CaII binding, but it unde...
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Published in | Biochemistry (Easton) Vol. 58; no. 2; pp. 120 - 125 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
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United States
American Chemical Society
15.01.2019
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Abstract | Lanmodulin (LanM) is a high-affinity lanthanide (Ln)-binding protein recently identified in Methylobacterium extorquens, a bacterium that requires Lns for the function of at least two enzymes. LanM possesses four EF-hands, metal coordination motifs generally associated with CaII binding, but it undergoes a metal-dependent conformational change with a 100 million-fold selectivity for LnIIIs and YIII over CaII. Here we present the nuclear magnetic resonance solution structure of LanM complexed with YIII. This structure reveals that LanM features an unusual fusion of adjacent EF-hands, resulting in a compact fold to the best of our knowledge unique among EF-hand-containing proteins. It also supports the importance of an additional carboxylate ligand in contributing to the protein’s picomolar affinity for LnIIIs, and it suggests a role of unusual N i+1–H···N i hydrogen bonds, in which LanM’s unique EF-hand proline residues are engaged, in selective LnIII recognition. This work sets the stage for a detailed mechanistic understanding of LanM’s Ln selectivity, which may inspire new strategies for binding, detecting, and sequestering these technologically important metals. |
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AbstractList | Lanmodulin (LanM) is a high-affinity lanthanide (Ln)-binding protein recently identified in Methylobacterium extorquens, a bacterium that requires Lns for the function of at least two enzymes. LanM possesses four EF-hands, metal coordination motifs generally associated with CaII binding, but it undergoes a metal-dependent conformational change with a 100 million-fold selectivity for LnIIIs and YIII over CaII. Here we present the nuclear magnetic resonance solution structure of LanM complexed with YIII. This structure reveals that LanM features an unusual fusion of adjacent EF-hands, resulting in a compact fold to the best of our knowledge unique among EF-hand-containing proteins. It also supports the importance of an additional carboxylate ligand in contributing to the protein’s picomolar affinity for LnIIIs, and it suggests a role of unusual N i+1–H···N i hydrogen bonds, in which LanM’s unique EF-hand proline residues are engaged, in selective LnIII recognition. This work sets the stage for a detailed mechanistic understanding of LanM’s Ln selectivity, which may inspire new strategies for binding, detecting, and sequestering these technologically important metals. Lanmodulin (LanM) is a high-affinity lanthanide (Ln)-binding protein recently identified in Methylobacterium extorquens, a bacterium that requires Lns for the function of at least two enzymes. LanM possesses four EF-hands, metal coordination motifs generally associated with Ca binding, but it undergoes a metal-dependent conformational change with a 100 million-fold selectivity for Ln s and Y over Ca . Here we present the nuclear magnetic resonance solution structure of LanM complexed with Y . This structure reveals that LanM features an unusual fusion of adjacent EF-hands, resulting in a compact fold to the best of our knowledge unique among EF-hand-containing proteins. It also supports the importance of an additional carboxylate ligand in contributing to the protein's picomolar affinity for Ln s, and it suggests a role of unusual N -H···N hydrogen bonds, in which LanM's unique EF-hand proline residues are engaged, in selective Ln recognition. This work sets the stage for a detailed mechanistic understanding of LanM's Ln selectivity, which may inspire new strategies for binding, detecting, and sequestering these technologically important metals. |
Author | Showalter, Scott A Cotruvo, Joseph A Featherston, Emily R Cook, Erik C |
AuthorAffiliation | Department of Chemistry Department of Biochemistry and Molecular Biology |
AuthorAffiliation_xml | – name: Department of Chemistry – name: Department of Biochemistry and Molecular Biology |
Author_xml | – sequence: 1 givenname: Erik C surname: Cook fullname: Cook, Erik C organization: Department of Chemistry – sequence: 2 givenname: Emily R surname: Featherston fullname: Featherston, Emily R organization: Department of Chemistry – sequence: 3 givenname: Scott A orcidid: 0000-0001-5179-032X surname: Showalter fullname: Showalter, Scott A email: sas76@psu.edu organization: Department of Biochemistry and Molecular Biology – sequence: 4 givenname: Joseph A orcidid: 0000-0003-4243-8257 surname: Cotruvo fullname: Cotruvo, Joseph A email: juc96@psu.edu organization: Department of Chemistry |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/30352145$$D View this record in MEDLINE/PubMed |
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Title | Structural Basis for Rare Earth Element Recognition by Methylobacterium extorquens Lanmodulin |
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