Structural highlights
Function
Q8ZPY6_SALTY
Publication Abstract from PubMed
Small heat shock proteins are ubiquitous molecular chaperones that form the first line of defence against the detrimental effects of cellular stress. Under conditions of stress they undergo drastic conformational rearrangements in order to bind to misfolded substrate proteins and prevent cellular protein aggregation. Owing to the dynamic nature of small heat shock protein oligomers, elucidating the structural basis of chaperone action and oligomerization still remains a challenge. In order to understand the organization of sHSP oligomers, we have determined crystal structures of a small heat shock protein from Salmonella typhimurium in a dimeric form and two higher oligomeric forms: an 18-mer and a 24-mer. Though the core dimer structure is conserved in all the forms, structural heterogeneity arises due to variation in the terminal regions.
Multiple oligomeric structures of a bacterial small heat shock protein.,Mani N, Bhandari S, Moreno R, Hu L, Prasad BV, Suguna K Sci Rep. 2016 Apr 7;6:24019. doi: 10.1038/srep24019. PMID:27053150[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mani N, Bhandari S, Moreno R, Hu L, Prasad BV, Suguna K. Multiple oligomeric structures of a bacterial small heat shock protein. Sci Rep. 2016 Apr 7;6:24019. doi: 10.1038/srep24019. PMID:27053150 doi:http://dx.doi.org/10.1038/srep24019
