PDBsum entry: 1t7s

Chaperone

PDB id: 1t7s

Contents

Protein chains

129 a.a. *

Waters ×50

* Residue conservation analysis

PDB id:

1t7s

Name:

Chaperone

Title:

Structural genomics of caenorhabditis elegans: structure of bag-1 protein

Structure:

Bag-1 cochaperone. Chain: a, b. Fragment: residues 74-210. Synonym: human bag1 homolog, bcl-2 binding athanogene. Engineered: yes. Mutation: yes

Source:

Caenorhabditis elegans. Organism_taxid: 6239. Gene: bag-1. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PQS)

Resolution:

2.80Å R-factor: 0.224 R-free: 0.298

Authors:

J.Symersky,Y.Zhang,N.Schormann,S.Li,R.Bunzel,P.Pruett,C.- H.Luan,M.Luo,Southeast Collaboratory For Structural Genomics (Secsg)

Key ref:

J.Symersky et al. (2004). Structural genomics of Caenorhabditis elegans: structure of the BAG domain. Acta Crystallogr D Biol Crystallogr, 60, 1606-1610. PubMed id: 15333932 DOI: 10.1107/S0907444904017603

Date:

10-May-04 Release date: 18-May-04

Protein chains

O44739  (BAG1_CAEEL) -  BAG family molecular chaperone regulator 1

Seq: 210 a.a.

Struc: 129 a.a.

 Gene Ontology (GO) functional annotation 

• Biochemical function: chaperone binding (1 term)

DOI no: 10.1107/S0907444904017603

Acta Crystallogr D Biol Crystallogr 60:1606-1610 (2004)

PubMed id: 15333932

Structural genomics of Caenorhabditis elegans: structure of the BAG domain.

J.Symersky, Y.Zhang, N.Schormann, S.Li, R.Bunzel, P.Pruett, C.H.Luan, M.Luo.

ABSTRACT

Binding of the BAG domain to the eukaryotic chaperone heat-shock protein (Hsp70) promotes ATP-dependent release of the protein substrate from Hsp70. Although the murine and human BAG domains have been shown to form an antiparallel three-helix bundle, the Caenorhabditis elegans BAG domain is formed by two antiparallel helices, while the third helix is extended away and stabilized by crystal-packing interactions. A small beta-sheet between helices 2 and 3 interferes with formation of the intramolecular three-helix bundle. However, intermolecular three-helix bundles are observed throughout the crystal packing and suggest that stable functional dimers and tetramers can be formed in solution. The structure may represent a new folding type of the BAG domain.

Selected figure(s)

Figure 1.
Figure 1 Ribbon representation of the two chains from the asymmetric unit of the crystal structure of the BAG domain from C. elegans. Rendered using MOLMOL (Koradi et al., 1996[Koradi, R., Billeter, M. & Wuthrich, K. (1996). J. Mol. Graph. 14, 51-55.]).

Figure 2.
Figure 2 Superimpositions of the BAG domain from C. elegans chain A (cyan), with (a) the human BAG domain (gold) and (b) murine BAG domain (yellow) through the corresponding helices 1 and 2. The helices are represented by cylinders and the -strands by arrows. The superimpositions were made using the program TOPP from the CCP4 suite (Collaborative Computational Project, Number 4, 1994[Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50, 760-763.]). The figures were prepared in Viewer Lite 5.0 (Accelrys).

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2004, 60, 1606-1610) copyright 2004.

Figures were selected by an automated process.