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1i42
From Proteopedia
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(New page: 200px<br /><applet load="1i42" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i42" /> '''NMR STRUCTURE OF THE UBX DOMAIN FROM P47'''<...)
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Revision as of 14:55, 20 November 2007
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NMR STRUCTURE OF THE UBX DOMAIN FROM P47
Overview
p47 is the major protein identified in complex with the cytosolic AAA, ATPase p97. It functions as an essential cofactor of p97-regulated, membrane fusion, which has been suggested to disassemble t-t-SNARE, complexes and prepare them for further rounds of membrane fusion. Here, we, report the high-resolution NMR structure of the C-terminal domain from, p47. It comprises a UBX domain and a 13 residue long structured N-terminal, extension. The UBX domain adopts a characteristic ubiquitin fold with a, betabetaalphabetabetaalphabeta secondary structure arrangement. Three, hydrophobic residues from the N-terminal extension pack closely against a, cleft in the UBX domain. We also identify, for the first time, the p97, interaction surface using NMR chemical shift perturbation studies.
About this Structure
1I42 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Solution structure and interaction surface of the C-terminal domain from p47: a major p97-cofactor involved in SNARE disassembly., Yuan X, Shaw A, Zhang X, Kondo H, Lally J, Freemont PS, Matthews S, J Mol Biol. 2001 Aug 10;311(2):255-63. PMID:11478859
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