6JZB

Structural characterization of DnaJ from Streptococcus pneumonia presents a new tetramer of Hsp40 family

Summary for 6JZB

• Entry DOI: 10.2210/pdb6jzb/pdb
• Descriptor: Chaperone protein DnaJ, ZINC ION (2 entities in total)
• Functional Keywords: cochaperone activity, zinc finger, tetramer, structural protein
• Biological source: Streptococcus pneumoniae
• Total number of polymer chains: 1
• Total formula weight: 41574.71

Authors

Zhu, M.,Zhu, Z.L. (deposition date: 2019-04-30, release date: 2020-11-04, Last modification date: 2024-03-27)

Primary citation

Zhu, M.,Ou, D.,Khan, M.H.,Zhao, S.,Zhu, Z.,Niu, L.
Structural insights into the formation of oligomeric state by a type I Hsp40 chaperone.
Biochimie, 176:45-51, 2020

PubMed Abstract: Molecular chaperones can prevent and repair protein misfolding and aggregation to maintain protein homeostasis in cells. Hsp40 chaperones interact with unfolded client proteins via the dynamic multivalent interaction (DMI) mechanism with their multiple client-binding sites. Here we report that a type I Hsp40 chaperone from Streptococcus pneumonia (spHsp40) forms a concentration-independent polydispersity oligomer state in solution. The crystal structure of spHsp40 determined at 2.75 Å revealed that each monomer has a type I Hsp40 structural fold containing a zinc finger domain and C-terminal domains I and II (CTD I and CTD II). Subsequent quaternary structure analysis using a PISA server generated two dimeric models. The interface mutational analysis suggests the conserved C-terminal dimeric motif as a basis for dimer formation and that the novel dimeric interaction between a client-binding site in CTD I and the zinc finger domain promotes the formation of the spHsp40 oligomeric state. In vitro functional analysis demonstrated that spHsp40 oligomer is fully active and possess the optimal activity in stimulating the ATPase activity of spHsp70. The oligomer state of type I Hsp40 and its formation might be important in understanding Hsp40 function and its interaction with client proteins.

PubMed: 32621942
DOI: 10.1016/j.biochi.2020.06.009

Experimental method

X-RAY DIFFRACTION (2.754 Å)