1i42
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i42 OCA], [http://www.ebi.ac.uk/pdbsum/1i42 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i42 RCSB]</span> | ||
}} | }} | ||
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[[Category: unusual n-terminal feature]] | [[Category: unusual n-terminal feature]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:14:20 2008'' |
Revision as of 18:14, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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