PDBsum entry 2d9d

Chaperone

PDB id: 2d9d

Contents

Protein chain

89 a.a.

PDB id:

2d9d

Name:

Chaperone

Title:

Solution structure of the bag domain (275-350) of bag-family molecular chaperone regulator-5

Structure:

Bag family molecular chaperone regulator 5. Chain: a. Fragment: bag domain. Synonym: bcl2-associated athanogene 5, bag-5. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: bag5. Expressed in: cell free protein synthesis.

NMR struc:

20 models

Authors:

R.Hatta,F.Hayashi,M.Yoshida,S.Yokoyama,Riken Structural Genomics/proteomics Initiative (Rsgi)

Key ref:

A.Arakawa et al. (2010). The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange. Structure, 18, 309-319. PubMed id: 20223214

Date:

09-Dec-05 Release date: 09-Dec-06

Protein chain

Q9UL15  (BAG5_HUMAN) -  BAG family molecular chaperone regulator 5 from Homo sapiens

Seq: 447 a.a.

Struc: 89 a.a.*

* PDB and UniProt seqs differ at 13 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

Structure 18:309-319 (2010)

PubMed id: 20223214

The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange.

A.Arakawa, N.Handa, N.Ohsawa, M.Shida, T.Kigawa, F.Hayashi, M.Shirouzu, S.Yokoyama.

ABSTRACT

ADP-ATP exchange by the molecular chaperone Hsp70 is enhanced by several cochaperones. BAG5 consists of five BAG domains and associates with the nucleotide-binding domain (NBD) of Hsp70. The overexpression of BAG5 in the cytosol reportedly disturbs Hsp70-mediated protein refolding and induces Parkinson's disease. In the present study, we found that the fifth BAG domain (BD5) of BAG5 is responsible for the interaction between Hsp70 and BAG5. We also determined the crystal structures of the BD5*NBD complex. BD5 binding caused two different types of NBD conformational changes, which both disrupted the nucleotide-binding groove. In fact, BD5 reduced the affinity of the NBD for ADP. Moreover, BD5, as well as the full-length BAG5, accelerated Hsp70-mediated refolding in an in vitro assay. Therefore, BAG5 can function as the nucleotide exchange factor of Hsp70 for the enhancement of protein refolding.