PDBsum entry 1vaz

Lipid binding protein

PDB id: 1vaz

Contents

Protein chain

76 a.a. *

* Residue conservation analysis

PDB id:

1vaz

Name:

Lipid binding protein

Title:

Solution structures of the p47 sep domain

Structure:

Nsfl1 cofactor p47. Chain: a. Fragment: p47 sep domain (residues 1-76). Synonym: p97 cofactor p47, xy body-associated protein xy40. Engineered: yes

Source:

Rattus norvegicus. Norway rat. Organism_taxid: 10116. Tissue: liver. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

10 models

Authors:

X.Yuan,P.Simpson,C.Mckeown,H.Kondo,K.Uchiyama,R.Wallis,I.Dreveny, C.Keetch,X.Zhang,C.Robinson,P.Freemont,S.Matthews

Key ref:

X.Yuan et al. (2004). Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97. EMBO J, 23, 1463-1473. PubMed id: 15029246 DOI: 10.1038/sj.emboj.7600152

Date:

20-Feb-04 Release date: 06-Apr-04

Protein chain

O35987  (NSF1C_RAT) -  NSFL1 cofactor p47 from Rattus norvegicus

Seq: 370 a.a.

Struc: 76 a.a.

DOI no: 10.1038/sj.emboj.7600152

EMBO J 23:1463-1473 (2004)

PubMed id: 15029246

Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97.

X.Yuan, P.Simpson, C.McKeown, H.Kondo, K.Uchiyama, R.Wallis, I.Dreveny, C.Keetch, X.Zhang, C.Robinson, P.Freemont, S.Matthews.

ABSTRACT

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.

Selected figure(s)

Figure 1.
Figure 1 Schematic representation of the domain structure of full-length rat p47 and fragments used in this study.

Figure 4.
Figure 4 Comparison of p47 UBA -ubiquitin, CUE -ubiquitin and di-ubiquitin structures. (A) C[ ]traces representing the superimposition of the 10 refined p47 UBA -ubiquitin complex structures using the HADDOCK approach. p47 UBA is shown in gold and ubiquitin in green. (B) Ribbon representation of the p47 UBA -ubiquitin complex. (C) Ribbon representation of the structure of the yeast CUE2-1 domain -ubiquitin complex in the same orientation as in (B). The CUE domain is shown in purple (Kang et al, 2003; Shih et al, 2003). (D) Ribbon representation of the structure of Lys48-linked di-ubiquitin in the same orientation as in (B) (Cook et al, 1992, 1994; Cummings et al, 1995; Beal et al, 1998; Phillips et al, 2001; Varadan et al, 2002).

The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (2004, 23, 1463-1473) copyright 2004.

Figures were selected by an automated process.