1xwi
From Proteopedia
(New page: 200px<br /> <applet load="1xwi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xwi, resolution 2.80Å" /> '''Crystal Structure o...) |
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| - | [[Image:1xwi.gif|left|200px]]<br /> | + | [[Image:1xwi.gif|left|200px]]<br /><applet load="1xwi" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1xwi" size=" | + | |
caption="1xwi, resolution 2.80Å" /> | caption="1xwi, resolution 2.80Å" /> | ||
'''Crystal Structure of VPS4B'''<br /> | '''Crystal Structure of VPS4B'''<br /> | ||
==Overview== | ==Overview== | ||
| - | VPS4 ATPases function in multivesicular body formation and in HIV-1 | + | VPS4 ATPases function in multivesicular body formation and in HIV-1 budding. Here, we report the crystal structure of monomeric apo human VPS4B/SKD1 (hVPS4B), which is composed of five distinct elements: a poorly ordered N-terminal MIT domain that binds ESCRT-III substrates, large (mixed alpha/beta) and small (alpha) AAA ATPase domains that closely resemble analogous domains in the p97 D1 ATPase cassette, a three-stranded antiparallel beta domain inserted within the small ATPase domain, and a novel C-terminal helix. Apo hVPS4B and yeast Vps4p (yVps4p) proteins dimerized in solution, and assembled into larger complexes (10-12 subunits) upon ATP binding. Human and yeast adaptor proteins (LIP5 and yVta1p, respectively) bound the beta domains of the fully assembled hVPS4B and yVps4p proteins. We therefore propose that Vps4 proteins cycle between soluble, inactive low molecular weight complexes and active, membrane-associated double-ring structures that bind ATP and coassemble with LIP5/Vta1. Finally, HIV-1 budding was inhibited by mutations in a loop that projects into the center of the modeled hVPS4B rings, suggesting that hVPS4B may release the assembled ESCRT machinery by pulling ESCRT-III substrates up into the central pore. |
==About this Structure== | ==About this Structure== | ||
| - | 1XWI 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 SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1XWI 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=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XWI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Hill, C | + | [[Category: Hill, C P.]] |
[[Category: Scott, A.]] | [[Category: Scott, A.]] | ||
| - | [[Category: Sundquist, W | + | [[Category: Sundquist, W I.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: aaa atpase]] | [[Category: aaa atpase]] | ||
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[[Category: vps4b]] | [[Category: vps4b]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:59:20 2008'' |
Revision as of 13:59, 21 February 2008
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Crystal Structure of VPS4B
Overview
VPS4 ATPases function in multivesicular body formation and in HIV-1 budding. Here, we report the crystal structure of monomeric apo human VPS4B/SKD1 (hVPS4B), which is composed of five distinct elements: a poorly ordered N-terminal MIT domain that binds ESCRT-III substrates, large (mixed alpha/beta) and small (alpha) AAA ATPase domains that closely resemble analogous domains in the p97 D1 ATPase cassette, a three-stranded antiparallel beta domain inserted within the small ATPase domain, and a novel C-terminal helix. Apo hVPS4B and yeast Vps4p (yVps4p) proteins dimerized in solution, and assembled into larger complexes (10-12 subunits) upon ATP binding. Human and yeast adaptor proteins (LIP5 and yVta1p, respectively) bound the beta domains of the fully assembled hVPS4B and yVps4p proteins. We therefore propose that Vps4 proteins cycle between soluble, inactive low molecular weight complexes and active, membrane-associated double-ring structures that bind ATP and coassemble with LIP5/Vta1. Finally, HIV-1 budding was inhibited by mutations in a loop that projects into the center of the modeled hVPS4B rings, suggesting that hVPS4B may release the assembled ESCRT machinery by pulling ESCRT-III substrates up into the central pore.
About this Structure
1XWI is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Structural and mechanistic studies of VPS4 proteins., Scott A, Chung HY, Gonciarz-Swiatek M, Hill GC, Whitby FG, Gaspar J, Holton JM, Viswanathan R, Ghaffarian S, Hill CP, Sundquist WI, EMBO J. 2005 Oct 19;24(20):3658-69. Epub 2005 Sep 29. PMID:16193069
Page seeded by OCA on Thu Feb 21 15:59:20 2008
Categories: Homo sapiens | Single protein | Hill, C P. | Scott, A. | Sundquist, W I. | SO4 | Aaa atpase | Skd1 | Vps4b
