2g3k
From Proteopedia
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| - | [[Image:2g3k.gif|left|200px]] | + | [[Image:2g3k.gif|left|200px]] |
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| - | '''Crystal structure of the C-terminal domain of Vps28''' | + | {{Structure |
| + | |PDB= 2g3k |SIZE=350|CAPTION= <scene name='initialview01'>2g3k</scene>, resolution 3.05Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= VPS28 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the C-terminal domain of Vps28''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2G3K is a [ | + | 2G3K is a [[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=2G3K OCA]. |
==Reference== | ==Reference== | ||
| - | The crystal structure of the C-terminal domain of Vps28 reveals a conserved surface required for Vps20 recruitment., Pineda-Molina E, Belrhali H, Piefer AJ, Akula I, Bates P, Weissenhorn W, Traffic. 2006 Aug;7(8):1007-16. Epub 2006 Jun 2. PMID:[http:// | + | The crystal structure of the C-terminal domain of Vps28 reveals a conserved surface required for Vps20 recruitment., Pineda-Molina E, Belrhali H, Piefer AJ, Akula I, Bates P, Weissenhorn W, Traffic. 2006 Aug;7(8):1007-16. Epub 2006 Jun 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16749904 16749904] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: 4 helix bundle]] | [[Category: 4 helix bundle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:00:06 2008'' |
Revision as of 15:00, 20 March 2008
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| , resolution 3.05Å | |||||||
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| Gene: | VPS28 (Saccharomyces cerevisiae) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the C-terminal domain of Vps28
Overview
The endosomal sorting complex I required for transport (ESCRT-I) is composed of the three subunits Vps23/Tsg101, Vps28 and Vps37. ESCRT-I is recruited to cellular membranes during multivesicular endosome biogenesis and by enveloped viruses such as HIV-1 to mediate budding from the cell. Here, we describe the crystal structure of a conserved C-terminal domain from Sacharomyces cerevisiae Vps28 (Vps28-CTD) at 3.05 A resolution which folds independently into a four-helical bundle structure. Co-expression experiments of Vps28-CTD, Vps23 and Vps37 suggest that Vps28-CTD does not directly participate in ESCRT-I assembly and may thus act as an adaptor module for downstream interaction partners. We show through mutagenesis studies that Vps28-CTD employs its strictly conserved surface in the interaction with the ESCRT-III factor Vps20. Furthermore, we present evidence that Vps28-CTD is sufficient to rescue an equine infectious anaemia virus (EIAV) Gag late domain deletion. Vps28-CTD mutations abolishing Vps20 interaction in vitro also prevent the rescue of the EIAV Gag late domain mutant consistent with a potential direct Vps28-ESCRT-III Vps20 recruitment. Therefore, the physiological relevant EIAV Gag-Alix interaction can be functionally replaced by a Gag-Vps28-CTD fusion. Because both Alix and Vps28-CTD can directly recruit ESCRT-III proteins, ESCRT-III assembly coupled to Vps4 action may therefore constitute the minimal budding machinery for EIAV release.
About this Structure
2G3K is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
The crystal structure of the C-terminal domain of Vps28 reveals a conserved surface required for Vps20 recruitment., Pineda-Molina E, Belrhali H, Piefer AJ, Akula I, Bates P, Weissenhorn W, Traffic. 2006 Aug;7(8):1007-16. Epub 2006 Jun 2. PMID:16749904
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