2d2s
From Proteopedia
(New page: 200px<br /><applet load="2d2s" size="450" color="white" frame="true" align="right" spinBox="true" caption="2d2s, resolution 2.85Å" /> '''Crystal Structure of...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2d2s.jpg|left|200px]]<br /><applet load="2d2s" size=" | + | [[Image:2d2s.jpg|left|200px]]<br /><applet load="2d2s" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2d2s, resolution 2.85Å" /> | caption="2d2s, resolution 2.85Å" /> | ||
'''Crystal Structure of the Exo84p C-terminal Domains'''<br /> | '''Crystal Structure of the Exo84p C-terminal Domains'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The exocyst is a large complex that is required for tethering vesicles at | + | The exocyst is a large complex that is required for tethering vesicles at the final stages of the exocytic pathway in all eukaryotes. Here we present the structures of the Exo70p subunit of this complex and of the C-terminal domains of Exo84p, at 2.0-A and 2.85-A resolution, respectively. Exo70p forms a 160-A-long rod with a novel fold composed of contiguous alpha-helical bundles. The Exo84p C terminus also forms a long rod (80 A), which unexpectedly has the same fold as the Exo70p N terminus. Our structural results and our experimental observations concerning the interaction between Exo70p and other exocyst subunits or Rho3p GTPase are consistent with an architecture wherein exocyst subunits are composed of mostly helical modules strung together into long rods. |
==About this Structure== | ==About this Structure== | ||
| - | 2D2S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http:// | + | 2D2S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D2S OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Dong, G.]] | [[Category: Dong, G.]] | ||
[[Category: Fu, C.]] | [[Category: Fu, C.]] | ||
| - | [[Category: Hutagalung, A | + | [[Category: Hutagalung, A H.]] |
[[Category: Novick, P.]] | [[Category: Novick, P.]] | ||
| - | [[Category: Reinisch, K | + | [[Category: Reinisch, K M.]] |
[[Category: exo84p]] | [[Category: exo84p]] | ||
[[Category: exocyst]] | [[Category: exocyst]] | ||
[[Category: tethering complex]] | [[Category: tethering complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:48 2008'' |
Revision as of 14:54, 21 February 2008
|
Crystal Structure of the Exo84p C-terminal Domains
Overview
The exocyst is a large complex that is required for tethering vesicles at the final stages of the exocytic pathway in all eukaryotes. Here we present the structures of the Exo70p subunit of this complex and of the C-terminal domains of Exo84p, at 2.0-A and 2.85-A resolution, respectively. Exo70p forms a 160-A-long rod with a novel fold composed of contiguous alpha-helical bundles. The Exo84p C terminus also forms a long rod (80 A), which unexpectedly has the same fold as the Exo70p N terminus. Our structural results and our experimental observations concerning the interaction between Exo70p and other exocyst subunits or Rho3p GTPase are consistent with an architecture wherein exocyst subunits are composed of mostly helical modules strung together into long rods.
About this Structure
2D2S is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif., Dong G, Hutagalung AH, Fu C, Novick P, Reinisch KM, Nat Struct Mol Biol. 2005 Dec;12(12):1094-100. Epub 2005 Oct 26. PMID:16249794
Page seeded by OCA on Thu Feb 21 16:54:48 2008
