PDBsum entry 6ppt

Chaperone

PDB id: 6ppt

Contents

Protein chain

90 a.a.

PDB id:

6ppt

Name:

Chaperone

Title:

Structural basis for client recognition and activity of hsp40 chaperones

Structure:

Alkaline phosphatase,chaperone protein dnaj 2 fusion. Chain: a. Synonym: apase. Engineered: yes

Source:

Escherichia coli (strain k12), thermus thermophilus (strain hb8 / atcc 27634 / dsm 579). Organism_taxid: 83333, 300852. Strain: k12, hb8 / atcc 27634 / dsm 579. Gene: phoa, b0383, jw0374, dnaj2, ttha1489. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

20 models

Authors:

Y.Jiang,P.Rossi,C.G.Kalodimos

Key ref:

Y.Jiang et al. (2019). Structural basis for client recognition and activity of Hsp40 chaperones. Science, 365, 1313-1319. PubMed id: 31604242 DOI: 10.1126/science.aax1280

Date:

08-Jul-19 Release date: 18-Sep-19

Protein chain

P00634  (PPB_ECOLI) -  Alkaline phosphatase from Escherichia coli (strain K12)

Seq: 471 a.a.

Struc: 90 a.a.*

Protein chain

Q56237  (DNAJ2_THET8) -  Chaperone protein DnaJ 2 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

Seq: 280 a.a.

Struc: 90 a.a.*

* PDB and UniProt seqs differ at 92 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.1.3.1 - alkaline phosphatase.
• Reaction: a phosphate monoester + H2O = an alcohol + phosphate
• Cofactor: Mg(2+); Zn(2+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1126/science.aax1280

Science 365:1313-1319 (2019)

PubMed id: 31604242

Structural basis for client recognition and activity of Hsp40 chaperones.

Y.Jiang, P.Rossi, C.G.Kalodimos.

ABSTRACT

Hsp70 and Hsp40 chaperones work synergistically in a wide range of biological processes including protein synthesis, membrane translocation, and folding. We used nuclear magnetic resonance spectroscopy to determine the solution structure and dynamic features of an Hsp40 in complex with an unfolded client protein. Atomic structures of the various binding sites in the client complexed to the binding domains of the Hsp40 reveal the recognition pattern. Hsp40 engages the client in a highly dynamic fashion using a multivalent binding mechanism that alters the folding properties of the client. Different Hsp40 family members have different numbers of client-binding sites with distinct sequence selectivity, providing additional mechanisms for activity regulation and function modification. Hsp70 binding to Hsp40 displaces the unfolded client. The activity of Hsp40 is altered in its complex with Hsp70, further regulating client binding and release.