ISDA: 1VAZ

Deposition Date 2004-02-20

Release Date 2004-04-06

Last Version Date 2023-12-27

Entry Detail

PDB ID:

1VAZ

Keywords:

LIPID BINDING PROTEIN

Title:

Solution structures of the p47 SEP domain

Biological Source:

Source Organism(s):

Rattus norvegicus (Taxon ID: 10116)

Expression System(s):

Escherichia coli

Method Details:

Experimental Method:

SOLUTION NMR

Conformers Calculated:

100

Conformers Submitted:

Selection Criteria:

structures with acceptable covalent geometry, structures with favorable non-bond energy, structures with the least restraint violations, structures with the lowest energy

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Macromolecular Entities

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:NSFL1 cofactor p47
Gene (Uniprot):Nsfl1c
Chain IDs:A
Chain Length:88
Number of Molecules:1
Biological Source:Rattus norvegicus

UniProt ID:O35987 Pfam ID:PF08059

Ligand Molecules

Primary Citation

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.Show

EMBO J. 23 1463 1473 (2004)

PMID: 15029246 DOI: 10.1038/sj.emboj.7600152

Abstact

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.

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Primary Citation of related structures

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