4yl9

Crystal Structure of wild-type of hsp14.1 from Sulfolobus solfatataricus P2

spinqualitylabelsall models 4yl9, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4yl9 is a 4 chain structure with sequence from Saccharolobus solfataricus 98/2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.353Å Ligands: CA, EDO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D0KNS6_SACS9 Publication Abstract from PubMed 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. Active-State Structures of a Small Heat-Shock Protein Revealed a Molecular Switch for Chaperone Function.,Liu L, Chen JY, Yang B, Wang FH, Wang YH, Yun CH Structure. 2015 Nov 3;23(11):2066-75. doi: 10.1016/j.str.2015.08.015. Epub 2015, Oct 1. PMID:26439766 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Heat Shock Protein structures

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