2a2f
From Proteopedia
(New page: 200px<br /><applet load="2a2f" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a2f, resolution 2.50Å" /> '''Crystal Structure of...) |
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| - | [[Image:2a2f.gif|left|200px]]<br /><applet load="2a2f" size=" | + | [[Image:2a2f.gif|left|200px]]<br /><applet load="2a2f" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2a2f, resolution 2.50Å" /> | caption="2a2f, resolution 2.50Å" /> | ||
'''Crystal Structure of Sec15 C-terminal domain'''<br /> | '''Crystal Structure of Sec15 C-terminal domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Sec15, a component of the exocyst, recognizes vesicle-associated Rab | + | Sec15, a component of the exocyst, recognizes vesicle-associated Rab GTPases, helps target transport vesicles to the budding sites in yeast and is thought to recruit other exocyst proteins. Here we report the characterization of a 35-kDa fragment that comprises most of the C-terminal half of Drosophila melanogaster Sec15. This C-terminal domain was found to bind a subset of Rab GTPases, especially Rab11, in a GTP-dependent manner. We also provide evidence that in fly photoreceptors Sec15 colocalizes with Rab11 and that loss of Sec15 affects rhabdomere morphology. Determination of the 2.5-A crystal structure of the C-terminal domain revealed a novel fold consisting of ten alpha-helices equally distributed between two subdomains (N and C subdomains). We show that the C subdomain, mainly via a single helix, is sufficient for Rab binding. |
==About this Structure== | ==About this Structure== | ||
| - | 2A2F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http:// | + | 2A2F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A2F OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bellen, H | + | [[Category: Bellen, H J.]] |
| - | [[Category: Mehta, S | + | [[Category: Mehta, S Q.]] |
[[Category: Pichaud, F.]] | [[Category: Pichaud, F.]] | ||
| - | [[Category: Quiocho, F | + | [[Category: Quiocho, F A.]] |
[[Category: Wu, S.]] | [[Category: Wu, S.]] | ||
[[Category: all helical structure]] | [[Category: all helical structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:22:55 2008'' |
Revision as of 14:22, 21 February 2008
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Crystal Structure of Sec15 C-terminal domain
Overview
Sec15, a component of the exocyst, recognizes vesicle-associated Rab GTPases, helps target transport vesicles to the budding sites in yeast and is thought to recruit other exocyst proteins. Here we report the characterization of a 35-kDa fragment that comprises most of the C-terminal half of Drosophila melanogaster Sec15. This C-terminal domain was found to bind a subset of Rab GTPases, especially Rab11, in a GTP-dependent manner. We also provide evidence that in fly photoreceptors Sec15 colocalizes with Rab11 and that loss of Sec15 affects rhabdomere morphology. Determination of the 2.5-A crystal structure of the C-terminal domain revealed a novel fold consisting of ten alpha-helices equally distributed between two subdomains (N and C subdomains). We show that the C subdomain, mainly via a single helix, is sufficient for Rab binding.
About this Structure
2A2F is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivo., Wu S, Mehta SQ, Pichaud F, Bellen HJ, Quiocho FA, Nat Struct Mol Biol. 2005 Oct;12(10):879-85. Epub 2005 Sep 11. PMID:16155582
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