Mani, Nandini and Bhandari, Spraha and Moreno, Rodolfo and Hu, Liya and Prasad, Venkataram BV and Suguna, Kaza (2016) Multiple oligomeric structures of a bacterial small heat shock protein. In: SCIENTIFIC REPORTS, 6 .
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Abstract
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.
| Item Type: | Journal Article |
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| Publication: | SCIENTIFIC REPORTS |
| Publisher: | NATURE PUBLISHING GROUP |
| Additional Information: | Copy right for this article belongs to the NATURE PUBLISHING GROUP, MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND |
| Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit |
| Date Deposited: | 11 May 2016 05:41 |
| Last Modified: | 11 May 2016 05:41 |
| URI: | http://eprints.iisc.ac.in/id/eprint/53768 |
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