期刊
STRUCTURE
卷 23, 期 11, 页码 2066-2075出版社
CELL PRESS
DOI: 10.1016/j.str.2015.08.015
关键词
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资金
- National Basic Research Program of China (973 Program) [2012CB917202]
- National Science Foundation of China [31270769]
- Ministry of Science and Technology of China [NCET-12-0013]
- National Science Funds for the Excellent Youth Scholars [31222043]
- fundamental Research Funds for the Central Universities [2014ZM0062]
Small heat-shock proteins (sHsps) maintain cellular homeostasis by binding to denatured client proteins to prevent aggregation. Numerous studies indicate that the N-terminal domain (NTD) of sHsps is responsible for binding to client proteins, but the binding mechanism and chaperone activity regulation remain elusive. Here, we report the crystal structures of the wild-type and mutants of an sHsp from Sulfolobus solfataricus representing the inactive and active state of this protein, respectively. All three structures reveal well-defined NTD, but their conformations are remarkably different. The mutant NTDs show disrupted helices presenting a reformed hydrophobic surface compatible with recognizing client proteins. Our functional data show that mutating key hydrophobic residues in this region drastically altered the chaperone activity of this sHsp. These data suggest a new model in which a molecular switch located in NTD facilitates conformational changes for client protein binding.
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