1v92
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(New page: 200px<br /><applet load="1v92" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v92" /> '''Solution structure of the UBA domain from p4...)
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Revision as of 02:23, 21 November 2007
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Solution structure of the UBA domain from p47, a major cofactor of the AAA ATPase p97
Overview
p47 is a major adaptor molecule of the cytosolic AAA ATPase p97. The, principal role of the p97-p47 complex is in regulation of membrane fusion, events. Mono-ubiquitin recognition by p47 has also been shown to be, crucial in the p97-p47-mediated Golgi membrane fusion events. Here, we, describe the high-resolution solution structures of the N-terminal UBA, domain and the central domain (SEP) from p47. The p47 UBA domain has the, characteristic three-helix bundle fold and forms a highly stable complex, with ubiquitin. We report the interaction surfaces of the two proteins and, present a structure for the p47 UBA-ubiquitin complex. The p47 SEP domain, adopts a novel fold with a betabetabetaalphaalphabeta secondary structure, arrangement, where beta4 pairs in a parallel fashion to beta1. Based on, biophysical studies, we demonstrate a clear propensity for the, self-association of p47. Furthermore, p97 N binding abolishes p47, self-association, revealing the potential interaction surfaces for, recognition of other domains within p97 or the substrate.
About this Structure
1V92 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97., Yuan X, Simpson P, McKeown C, Kondo H, Uchiyama K, Wallis R, Dreveny I, Keetch C, Zhang X, Robinson C, Freemont P, Matthews S, EMBO J. 2004 Apr 7;23(7):1463-73. Epub 2004 Mar 18. PMID:15029246
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