Large nucleotide-dependent conformational change in Rab28
Rab GTPases are essential regulators of membrane trafficking. We report crystal structures of Rab28 in the active (GppNHp-bound) and inactive (GDP-3′P-bound) forms at 1.5 and 1.1 Å resolution. Rab28 is a distant member of the Rab family. While the overall fold of Rab28 resembles that of other Rab GT...
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| Published in | FEBS letters Vol. 582; no. 29; pp. 4107 - 4111 |
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| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
England
Elsevier B.V
10.12.2008
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| Subjects | |
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| Abstract | Rab GTPases are essential regulators of membrane trafficking. We report crystal structures of Rab28 in the active (GppNHp-bound) and inactive (GDP-3′P-bound) forms at 1.5 and 1.1
Å resolution. Rab28 is a distant member of the Rab family. While the overall fold of Rab28 resembles that of other Rab GTPases, it undergoes a larger nucleotide-dependent conformational change than other members of this family. Added flexibility resulting from a double-glycine motif at the beginning of switch 2 might partially account for this observation. The double-glycine motif, which is conserved in the Arf family, only occurs in Rab28 and Rab7B of the Rab family, and may have a profound effect on their catalytic activities. |
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| AbstractList | Rab GTPases are essential regulators of membrane trafficking. We report crystal structures of Rab28 in the active (GppNHp-bound) and inactive (GDP-3'P-bound) forms at 1.5 and 1.1A resolution. Rab28 is a distant member of the Rab family. While the overall fold of Rab28 resembles that of other Rab GTPases, it undergoes a larger nucleotide-dependent conformational change than other members of this family. Added flexibility resulting from a double-glycine motif at the beginning of switch 2 might partially account for this observation. The double-glycine motif, which is conserved in the Arf family, only occurs in Rab28 and Rab7B of the Rab family, and may have a profound effect on their catalytic activities. Rab GTPases are essential regulators of membrane trafficking. We report crystal structures of Rab28 in the active (GppNHp-bound) and inactive (GDP-3′P-bound) forms at 1.5 and 1.1 Å resolution. Rab28 is a distant member of the Rab family. While the overall fold of Rab28 resembles that of other Rab GTPases, it undergoes a larger nucleotide-dependent conformational change than other members of this family. Added flexibility resulting from a double-glycine motif at the beginning of switch 2 might partially account for this observation. The double-glycine motif, which is conserved in the Arf family, only occurs in Rab28 and Rab7B of the Rab family, and may have a profound effect on their catalytic activities. Rab GTPases are essential regulators of membrane trafficking. We report crystal structures of Rab28 in the active (GppNHp-bound) and inactive (GDP-3'P-bound) forms at 1.5 and 1.1 {angstrom} resolution. Rab28 is a distant member of the Rab family. While the overall fold of Rab28 resembles that of other Rab GTPases, it undergoes a larger nucleotide-dependent conformational change than other members of this family. Added flexibility resulting from a double-glycine motif at the beginning of switch 2 might partially account for this observation. The double-glycine motif, which is conserved in the Arf family, only occurs in Rab28 and Rab7B of the Rab family, and may have a profound effect on their catalytic activities. Rab GTPases are essential regulators of membrane trafficking. We report crystal structures of Rab28 in the active (GppNHp-bound) and inactive (GDP-3′P-bound) forms at 1.5Å and 1.1Å resolution. Rab28 is a distant member of the Rab family. While the overall fold of Rab28 resembles that of other Rab GTPases, it undergoes a larger nucleotide-dependent conformational change than other members of this family. Added flexibility resulting from a double-glycine motif at the beginning of switch 2 might partially account for this observation. The double-glycine motif, which is conserved in the Arf family, only occurs in Rab28 and Rab7B of the Rab family, and may have a profound effect on their catalytic activities. Rab GTPases are essential regulators of membrane trafficking. We report crystal structures of Rab28 in the active (GppNHp‐bound) and inactive (GDP‐3′P‐bound) forms at 1.5 and 1.1 Å resolution. Rab28 is a distant member of the Rab family. While the overall fold of Rab28 resembles that of other Rab GTPases, it undergoes a larger nucleotide‐dependent conformational change than other members of this family. Added flexibility resulting from a double‐glycine motif at the beginning of switch 2 might partially account for this observation. The double‐glycine motif, which is conserved in the Arf family, only occurs in Rab28 and Rab7B of the Rab family, and may have a profound effect on their catalytic activities. |
| Author | Dominguez, Roberto Lee, Sung Haeng Baek, Kyuwon |
| AuthorAffiliation | a Department of Physiology, University of Pennsylvania School of Medicine, 3700 Hamilton Walk, A507 Richards Building, Philadelphia, PA 19104-6085, USA |
| AuthorAffiliation_xml | – name: a Department of Physiology, University of Pennsylvania School of Medicine, 3700 Hamilton Walk, A507 Richards Building, Philadelphia, PA 19104-6085, USA |
| Author_xml | – sequence: 1 givenname: Sung Haeng surname: Lee fullname: Lee, Sung Haeng organization: Department of Physiology, University of Pennsylvania School of Medicine, 3700 Hamilton Walk, A507 Richards Building, Philadelphia, PA 19104-6085, USA – sequence: 2 givenname: Kyuwon surname: Baek fullname: Baek, Kyuwon organization: Department of Physiology, University of Pennsylvania School of Medicine, 3700 Hamilton Walk, A507 Richards Building, Philadelphia, PA 19104-6085, USA – sequence: 3 givenname: Roberto surname: Dominguez fullname: Dominguez, Roberto email: droberto@mail.med.upenn.edu organization: Department of Physiology, University of Pennsylvania School of Medicine, 3700 Hamilton Walk, A507 Richards Building, Philadelphia, PA 19104-6085, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/19026641$$D View this record in MEDLINE/PubMed https://www.osti.gov/biblio/1006977$$D View this record in Osti.gov |
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| Copyright | 2008 Federation of European Biochemical Societies FEBS Letters 582 (2008) 1873-3468 © 2015 Federation of European Biochemical Societies |
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| Keywords | Rab GTPase family GDP-3′P GTP analog GppNHp Crystal structure |
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| Snippet | Rab GTPases are essential regulators of membrane trafficking. We report crystal structures of Rab28 in the active (GppNHp-bound) and inactive (GDP-3′P-bound)... Rab GTPases are essential regulators of membrane trafficking. We report crystal structures of Rab28 in the active (GppNHp‐bound) and inactive (GDP‐3′P‐bound)... Rab GTPases are essential regulators of membrane trafficking. We report crystal structures of Rab28 in the active (GppNHp-bound) and inactive (GDP-3'P-bound)... |
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| SubjectTerms | Amino Acid Sequence CONFORMATIONAL CHANGES CRYSTAL STRUCTURE Crystallography, X-Ray FLEXIBILITY GDP-3′P GTP analog GppNHp GTP-ASES Guanosine Diphosphate - chemistry Guanylyl Imidodiphosphate - chemistry Humans MATERIALS SCIENCE MEMBRANES Protein Conformation rab GTP-Binding Proteins - chemistry Rab GTPase family RESOLUTION |
| Title | Large nucleotide-dependent conformational change in Rab28 |
| URI | https://dx.doi.org/10.1016/j.febslet.2008.11.008 https://onlinelibrary.wiley.com/doi/abs/10.1016%2Fj.febslet.2008.11.008 https://www.ncbi.nlm.nih.gov/pubmed/19026641 https://search.proquest.com/docview/19661563 https://search.proquest.com/docview/69844167 https://www.osti.gov/biblio/1006977 https://pubmed.ncbi.nlm.nih.gov/PMC2741181 |
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