1e32: Difference between revisions

Revision as of 00:04, 1 July 2008

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File:1e32.png

Template:STRUCTURE 1e32

STRUCTURE OF THE N-TERMINAL DOMAIN AND THE D1 AAA DOMAIN OF MEMBRANE FUSION ATPASE P97STRUCTURE OF THE N-TERMINAL DOMAIN AND THE D1 AAA DOMAIN OF MEMBRANE FUSION ATPASE P97

Template:ABSTRACT PUBMED 11163219

About this StructureAbout this Structure

1E32 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the AAA ATPase p97., Zhang X, Shaw A, Bates PA, Newman RH, Gowen B, Orlova E, Gorman MA, Kondo H, Dokurno P, Lally J, Leonard G, Meyer H, van Heel M, Freemont PS, Mol Cell. 2000 Dec;6(6):1473-84. PMID:11163219

Page seeded by OCA on Tue Jul 1 00:04:01 2008

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OCA

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-'''STRUCTURE OF THE N-TERMINAL DOMAIN AND THE D1 AAA DOMAIN OF MEMBRANE FUSION ATPASE P97'''
+===STRUCTURE OF THE N-TERMINAL DOMAIN AND THE D1 AAA DOMAIN OF MEMBRANE FUSION ATPASE P97===
-==Overview==
+<!--
-p97, an abundant hexameric ATPase of the AAA family, is involved in homotypic membrane fusion. It is thought to disassemble SNARE complexes formed during the process of membrane fusion. Here, we report two structures: a crystal structure of the N-terminal and D1 ATPase domains of murine p97 at 2.9 A resolution, and a cryoelectron microscopy structure of full-length rat p97 at 18 A resolution. Together, these structures show that the D1 and D2 hexamers pack in a tail-to-tail arrangement, and that the N domain is flexible. A comparison with NSF D2 (ATP complex) reveals possible conformational changes induced by ATP hydrolysis. Given the D1 and D2 packing arrangement, we propose a ratchet mechanism for p97 during its ATP hydrolysis cycle.
+The line below this paragraph, {{ABSTRACT_PUBMED_11163219}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_11163219}}
 ==About this Structure==
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 [[Category: Atpase]]
 [[Category: Membrane fusion]]
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