1JRU
NMR STRUCTURE OF THE UBX DOMAIN FROM P47 (ENERGY MINIMISED AVERAGE)
Summary for 1JRU
| Entry DOI | 10.2210/pdb1jru/pdb |
| Related | 1I42 |
| NMR Information | BMRB: 5155,5874,5876 |
| Descriptor | p47 protein (1 entity in total) |
| Functional Keywords | ubiquitin superfold, ubx, unusual n-terminal feature, unknown function |
| Biological source | Rattus norvegicus (Norway rat) |
| Cellular location | Nucleus: O35987 |
| Total number of polymer chains | 1 |
| Total formula weight | 9901.34 |
| Authors | Yuan, X.M.,Shaw, A.,Zhang, X.D.,Kondo, H.,Lally, J.,Freemont, P.S.,Matthews, S.J. (deposition date: 2001-08-15, release date: 2001-08-17, Last modification date: 2024-05-22) |
| Primary citation | Yuan, X.,Shaw, A.,Zhang, X.,Kondo, H.,Lally, J.,Freemont, P.S.,Matthews, S. Solution structure and interaction surface of the C-terminal domain from p47: a major p97-cofactor involved in SNARE disassembly. J.Mol.Biol., 311:255-263, 2001 Cited by PubMed Abstract: 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. PubMed: 11478859DOI: 10.1006/jmbi.2001.4864 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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