2ffq
From Proteopedia
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|PDB= 2ffq |SIZE=350|CAPTION= <scene name='initialview01'>2ffq</scene>, resolution 1.78Å | |PDB= 2ffq |SIZE=350|CAPTION= <scene name='initialview01'>2ffq</scene>, resolution 1.78Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GSP:5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= RAB6B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= RAB6B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2fe4|2FE4]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ffq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ffq OCA], [http://www.ebi.ac.uk/pdbsum/2ffq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ffq RCSB]</span> | ||
}} | }} | ||
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[[Category: Kozielski, F.]] | [[Category: Kozielski, F.]] | ||
[[Category: Tcherniuk, S.]] | [[Category: Tcherniuk, S.]] | ||
| - | [[Category: GSP]] | ||
| - | [[Category: MG]] | ||
[[Category: protein-nucleotide complex]] | [[Category: protein-nucleotide complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:02:13 2008'' |
Revision as of 00:02, 31 March 2008
| |||||||
| , resolution 1.78Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | RAB6B (Homo sapiens) | ||||||
| Related: | 2FE4
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The crystal structure of human neuronal Rab6B in its active GTPgS-bound form
Overview
The Rab small G-protein family plays important roles in eukaryotes as regulators of vesicle traffic. In Rab proteins, the hydrolysis of GTP to GDP is coupled with association with and dissociation from membranes. Conformational changes related to their different nucleotide states determine their effector specificity. The crystal structure of human neuronal Rab6B was solved in its 'inactive' (with bound MgGDP) and 'active' (MgGTPgammaS-bound) forms to 2.3 and 1.8 A, respectively. Both crystallized in space group P2(1)2(1)2(1), with similar unit-cell parameters, allowing the comparison of both structures without packing artifacts. Conformational changes between the inactive GDP and active GTP-like state are observed mainly in the switch I and switch II regions, confirming their role as a molecular switch. Compared with other Rab proteins, additional changes are observed in the Rab6 subfamily-specific RabSF3 region that might contribute to the specificity of Rab6 for its different effector proteins.
About this Structure
2FFQ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The structure of human neuronal Rab6B in the active and inactive form., Garcia-Saez I, Tcherniuk S, Kozielski F, Acta Crystallogr D Biol Crystallogr. 2006 Jul;62(Pt 7):725-33. Epub 2006, Jun 20. PMID:16790928
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