PDBsum entry: 1m62

Chaperone

PDB id: 1m62

Contents

Protein chain

87 a.a. *

* Residue conservation analysis

PDB id:

1m62

Name:

Chaperone

Title:

Solution structure of the bag domain from bag4/sodd

Structure:

Bag-family molecular chaperone regulator-4. Chain: a. Fragment: bag domain (residues 371-457). Synonym: silencer of death domains. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: bag4/sodd. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

25 models

Authors:

K.Briknarova,S.Takayama,S.Homma,K.Baker,E.Cabezas,D.W.Hoyt, Z.Li,A.C.Satterthwait,K.R.Ely

Key ref:

K.Briknarová et al. (2002). BAG4/SODD protein contains a short BAG domain. J Biol Chem, 277, 31172-31178. PubMed id: 12058034 DOI: 10.1074/jbc.M202792200

Date:

11-Jul-02 Release date: 24-Jul-02

Protein chain

O95429  (BAG4_HUMAN) -  BAG family molecular chaperone regulator 4

Seq: 457 a.a.

Struc: 87 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 

• Biochemical function: chaperone binding (1 term)

DOI no: 10.1074/jbc.M202792200

J Biol Chem 277:31172-31178 (2002)

PubMed id: 12058034

BAG4/SODD protein contains a short BAG domain.

K.Briknarová, S.Takayama, S.Homma, K.Baker, E.Cabezas, D.W.Hoyt, Z.Li, A.C.Satterthwait, K.R.Ely.

ABSTRACT

BAG (Bcl-2-associated athanogene) proteins are molecular chaperone regulators that affect diverse cellular pathways. All members share a conserved motif, called the BAG domain (BD), which binds to Hsp70/Hsc70 family proteins and modulates their activity. We have determined the solution structure of BD from BAG4/SODD (silencer of death domains) by multidimensional nuclear magnetic resonance methods and compared it to the corresponding domain in BAG1 (Briknarová, K., Takayama, S., Brive, L., Havert, M. L., Knee, D. A., Velasco, J., Homma, S., Cabezas, E., Stuart, J., Hoyt, D. W., Satterthwait, A. C., Llinás, M., Reed, J. C., and Ely, K. R. (2001) Nat. Struct. Biol. 8, 349-352). The difference between BDs from these two BAG proteins is striking, and the structural comparison defines two subfamilies of mammalian BD-containing proteins. One subfamily includes the closely related BAG3, BAG4, and BAG5 proteins, and the other is represented by BAG1, which contains a structurally and evolutionarily distinct BD. BDs from both BAG1 and BAG4 are three-helix bundles; however, in BAG4, each helix in this bundle is three to four turns shorter than its counterpart in BAG1, which reduces the length of the domain by one-third. BAG4 BD thus represents a prototype of the minimal functional fragment that is capable of binding to Hsc70 and modulating its chaperone activity.

Selected figure(s)

Figure 4.
Fig. 4. Surface maps of BAG4 BD. In panels a and b, the solvent accessible surface of the domain is colored according to electrostatic potential. Areas with negative, positive, or neutral character are depicted in red, blue, or white, respectively. In panel a, the view is the same as in Fig. 2, with helices 2 and 3 and the Hsc70 binding site facing forward. In panel b, the molecule is rotated 180° around a vertical axis relative to the view in panel a, thus revealing the opposite side with helix 1 in front. In panels c and d, the surface is colored according to hydrophobicity. Yellow color intensity is proportional to increasing hydrophobic character, and the front and back views of the molecule are displayed as in panels a and b. Charged and hydrophobic residues are labeled in the appropriate panels.

Figure 5.
Fig. 5. A comparative gallery of BAG domains. Contact surfaces of BDs from BAG1, BAG3, BAG4, and BAG5 (columns 1-9), whose sequences are aligned in Fig. 2, are colored according to electrostatic potential (rows 1 and 2) and hydrophobicity (rows 3 and 4). Residues 99-210 of murine BAG1 (PDB ID 1I6Z), residues 99-205 of human BAG3 (PDB ID 1HX1), residues 376-457 of human BAG4, and corresponding residues from homology models of BAG3 and BAG5 BDs are shown. Coloring and orientation are the same as in Fig. 4 to permit direct comparison. Front views are shown in rows 1 and 3, whereas back views are presented in rows 2 and 4.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2002, 277, 31172-31178) copyright 2002.

Figures were selected by an automated process.