2v6x: Difference between revisions

Revision as of 12:16, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2v6x.png

Template:STRUCTURE 2v6x

STRACTURAL INSIGHT INTO THE INTERACTION BETWEEN ESCRT-III AND VPS4STRACTURAL INSIGHT INTO THE INTERACTION BETWEEN ESCRT-III AND VPS4

Template:ABSTRACT PUBMED 17928861

About this StructureAbout this Structure

2V6X is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for selective recognition of ESCRT-III by the AAA ATPase Vps4., Obita T, Saksena S, Ghazi-Tabatabai S, Gill DJ, Perisic O, Emr SD, Williams RL, Nature. 2007 Oct 11;449(7163):735-9. PMID:17928861

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OCA

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-'''STRACTURAL INSIGHT INTO THE INTERACTION BETWEEN ESCRT-III AND VPS4'''
+===STRACTURAL INSIGHT INTO THE INTERACTION BETWEEN ESCRT-III AND VPS4===
-==Overview==
+<!--
-The AAA+ ATPases are essential for various activities such as membrane trafficking, organelle biogenesis, DNA replication, intracellular locomotion, cytoskeletal remodelling, protein folding and proteolysis. The AAA ATPase Vps4, which is central to endosomal traffic to lysosomes, retroviral budding and cytokinesis, dissociates ESCRT complexes (the endosomal sorting complexes required for transport) from membranes. Here we show that, of the six ESCRT--related subunits in yeast, only Vps2 and Did2 bind the MIT (microtubule interacting and transport) domain of Vps4, and that the carboxy-terminal 30 residues of the subunits are both necessary and sufficient for interaction. We determined the crystal structure of the Vps2 C terminus in a complex with the Vps4 MIT domain, explaining the basis for selective ESCRT-III recognition. MIT helices alpha2 and alpha3 recognize a (D/E)xxLxxRLxxL(K/R) motif, and mutations within this motif cause sorting defects in yeast. Our crystal structure of the amino-terminal domain of an archaeal AAA ATPase of unknown function shows that it is closely related to the MIT domain of Vps4. The archaeal ATPase interacts with an archaeal ESCRT-III-like protein even though these organisms have no endomembrane system, suggesting that the Vps4/ESCRT-III partnership is a relic of a function that pre-dates the divergence of eukaryotes and Archaea.
+The line below this paragraph, {{ABSTRACT_PUBMED_17928861}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17928861 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17928861}}
 ==About this Structure==
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 [[Category: Vps4a]]
 [[Category: Vps4b]]
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