2fe4
From Proteopedia
(New page: 200px<br /> <applet load="2fe4" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fe4, resolution 2.3Å" /> '''The crystal structur...) |
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| - | [[Image:2fe4.gif|left|200px]]<br /> | + | [[Image:2fe4.gif|left|200px]]<br /><applet load="2fe4" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="2fe4, resolution 2.3Å" /> | caption="2fe4, resolution 2.3Å" /> | ||
'''The crystal structure of human neuronal Rab6B in its inactive GDP-bound form'''<br /> | '''The crystal structure of human neuronal Rab6B in its inactive GDP-bound form'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Rab small G-protein family plays important roles in eukaryotes as | + | 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== | ==About this Structure== | ||
| - | 2FE4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG, NO3 and GDP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2FE4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=NO3:'>NO3</scene> and <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FE4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protein-nucleotide complex]] | [[Category: protein-nucleotide complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:20:26 2008'' |
Revision as of 15:20, 21 February 2008
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The crystal structure of human neuronal Rab6B in its inactive GDP-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
2FE4 is a Single protein structure of sequence from Homo sapiens with , and as ligands. 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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