3aab | pdb_00003aab

Small heat shock protein hsp14.0 with the mutations of I120F and I122F in the form I crystal

spinqualitylabelsall models 3aab, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3aab 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. Ligands: GOL, IPA Related: 3aac Gene: ST1653 (SULTO) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Small heat shock proteins (sHsps), which are categorized into a class of molecular chaperones, bind and stabilize denatured proteins to prevent aggregation. The sHsps undergo transition between different oligomeric states to control their hydrophobicity. So far, only the structures of sHsps in large oligomeric states have been reported. Here we report the structure of StHsp14.0 from Sulfolobus tokodaii in the dimeric state, which is formed by means of a mutation at the C-terminal IXI/V motif. The dimer is the sole building block in two crystal forms, and the dimeric mode is the same as that in the large oligomers. The N-terminal helix has variety in its conformation. Furthermore, spectroscopic and biochemical experiments were performed to investigate the conformational variability at the N-terminus. The structural, dynamical and oligomeric properties suggest that chaperone activity of StHsp14.0 is mediated by partially dissolved oligomers. Dimer structure and conformational variability in the N-terminal region of an archaeal small heat shock protein, StHsp14.0.,Takeda K, Hayashi T, Abe T, Hirano Y, Hanazono Y, Yohda M, Miki K J Struct Biol. 2010 Dec 30. PMID:21195185 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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