Structural highlights
Function
CH60_ECOLI Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.[HAMAP-Rule:MF_00600] Essential for the growth of the bacteria and the assembly of several bacteriophages. Also plays a role in coupling between replication of the F plasmid and cell division of the cell.[HAMAP-Rule:MF_00600]
Publication Abstract from PubMed
The GroEL-GroES chaperonin complex is a bacterial protein folding system, functioning in an ATP-dependent manner. Upon ATP binding and hydrolysis, it undergoes multiple stages linked to substrate protein binding, folding and release. Structural methods helped to reveal several conformational states and provide more information about the chaperonin functional cycle. Here, using cryo-EM we resolved two nucleotide-bound structures of the bullet-shaped GroEL-GroES(1) complex at 3.4 A resolution. The main difference between them is the relative orientation of their apical domains. Both structures contain nucleotides in cis and trans GroEL rings; in contrast to previously reported bullet-shaped complexes where nucleotides were only present in the cis ring. Our results suggest that the bound nucleotides correspond to ADP, and that such a state appears at low ATP:ADP ratios.
Novel cryo-EM structure of an ADP-bound GroEL-GroES complex.,Kudryavtseva SS, Pichkur EB, Yaroshevich IA, Mamchur AA, Panina IS, Moiseenko AV, Sokolova OS, Muronetz VI, Stanishneva-Konovalova TB Sci Rep. 2021 Sep 14;11(1):18241. doi: 10.1038/s41598-021-97657-x. PMID:34521893[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kudryavtseva SS, Pichkur EB, Yaroshevich IA, Mamchur AA, Panina IS, Moiseenko AV, Sokolova OS, Muronetz VI, Stanishneva-Konovalova TB. Novel cryo-EM structure of an ADP-bound GroEL-GroES complex. Sci Rep. 2021 Sep 14;11(1):18241. PMID:34521893 doi:10.1038/s41598-021-97657-x
