3vql | pdb_00003vql

Small heat shock protein hsp14.0 of C-terminal deletion variant

spinqualitylabelsall models 3vql, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vql is a 2 chain structure with sequence from Sulto. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3aab, 3aac, 3vqk, 3vqm Gene: hsp14.0, ST1653 (SULTO) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The small heat shock proteins (sHsps), which are widely found in all domains of life, bind and stabilize denatured proteins to prevent aggregation. The sHsps exist as large oligomers that are composed of 9-40 subunits and control their chaperone activity by the transition of the oligomeric state. Though the oligomeric transition is important for the biological function of most sHsps, atomic details have not been elucidated. Here, we report crystal structures in both the 24-meric and dimeric states for an sHsp, StHsp14.0 from Sulfolobus tokodaii, in order to reveal changes upon the oligomeric transition. The results indicate that StHsp14.0 forms a spherical 24-mer with a diameter of 115 A. The diameter is defined by the inter-monomer angle in the dimer. The dimer structure in the dimeric state shows only small differences from that in the 24-meric state. Some significant differences are exclusively observed at the binding site for the C-terminus. Although a dimer has four interactive sites with neighboring dimers, the weakness of the respective interactions is indicated from the size-exclusion chromatography. The small structural changes imply an activation mechanism mediated by multiple weak interactions. Structural Studies on the Oligomeric Transition of a Small Heat Shock Protein, StHsp14.0.,Hanazono Y, Takeda K, Yohda M, Miki K J Mol Biol. 2012 May 18. PMID:22613762 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Heat Shock Proteins

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