1i42 | pdb_00001i42
NMR STRUCTURE OF THE UBX DOMAIN FROM P47
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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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