2g3k: Difference between revisions
New page: left|200px<br /><applet load="2g3k" size="450" color="white" frame="true" align="right" spinBox="true" caption="2g3k, resolution 3.05Å" /> '''Crystal structure of... |
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[[Image:2g3k.gif|left|200px]]<br /><applet load="2g3k" size=" | [[Image:2g3k.gif|left|200px]]<br /><applet load="2g3k" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2g3k, resolution 3.05Å" /> | caption="2g3k, resolution 3.05Å" /> | ||
'''Crystal structure of the C-terminal domain of Vps28'''<br /> | '''Crystal structure of the C-terminal domain of Vps28'''<br /> | ||
==Overview== | ==Overview== | ||
The endosomal sorting complex I required for transport (ESCRT-I) is | 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== | ==About this Structure== | ||
2G3K 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:// | 2G3K 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=2G3K OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Bates, P.]] | [[Category: Bates, P.]] | ||
[[Category: Belrhali, H.]] | [[Category: Belrhali, H.]] | ||
[[Category: Piefer, A | [[Category: Piefer, A J.]] | ||
[[Category: Pineda-Molina, E.]] | [[Category: Pineda-Molina, E.]] | ||
[[Category: Weissenhorn, W.]] | [[Category: Weissenhorn, W.]] | ||
[[Category: 4 helix bundle]] | [[Category: 4 helix bundle]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:27:44 2008'' | ||
Revision as of 18:27, 21 February 2008
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Crystal structure of the C-terminal domain of Vps28
OverviewOverview
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 StructureAbout this Structure
2G3K is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
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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