7cpl

Xylanase R from Bacillus sp. TAR-1

spinqualitylabelsall models 7cpl, resolution 1.52Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7cpl is a 1 chain structure with sequence from Bacillus sp. TAR1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.52Å Ligands: CA, MPD, NI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function XYNA_HALH5 Publication Abstract from PubMed The mechanism of thermostabilization of GH10 xylanase, XynR, from Bacillus sp. strain TAR-1 by the mutation of S92 to E was investigated. Thermodynamic analysis revealed that thermostabilization was driven by the decrease in entropy change of activation for thermal inactivation. Crystallographic analysis suggested that this mutation suppressed the fluctuation of the amino acid residues at position 92-95. Insight into the mechanism of thermostabilization of GH10 xylanase from Bacillus sp. strain TAR-1 by the mutation of S92 to E.,Suzuki M, Takita T, Kuwata K, Nakatani K, Li T, Katano Y, Kojima K, Mizutani K, Mikami B, Yatsunami R, Nakamura S, Yasukawa K Biosci Biotechnol Biochem. 2021 Feb 18;85(2):386-390. doi: 10.1093/bbb/zbaa003. PMID:33604642 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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