4kys | pdb_00004kys

Clostridium botulinum thiaminase I in complex with thiamin

spinqualitylabelsall models 4kys, resolution 2.18Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4kys is a 2 chain structure with sequence from Clob1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CIT, MG, VIB Gene: CLB_0812 (CLOB1) Activity: Thiamine pyridinylase, with EC number 2.5.1.2 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Thiaminases are responsible for the degradation of thiamin and its metabolites. Two classes of thiaminases have been identified based on their three-dimensional structures and in their requirements for a nucleophilic second substrate. While the reactions of several thiaminases have been characterized, the physiological role of thiamin degradation is not fully understood. We have determined the three-dimensional X-ray structure of an inactive C143S mutant of Clostridium botulinum (Cb) thiaminase I with bound thiamin at 2.2 A resolution. The C143S/thiamin complex provides atomic level details of the orientation of thiamin upon binding to Cb-thiaminase I and the identity of active site residues involved in substrate binding and catalysis. The specific roles of active site residues were probed using site directed mutagenesis and kinetic analyses, leading to a detailed mechanism for Cb-thiaminase I. The structure of Cb-thiaminase I is also compared to the functionally similar but structurally distinct thiaminase II. Structure of a Clostridium botulinum C143S thiaminase I/thiamin complex reveals active site architecture.,Sikowitz MD, Shome B, Begley TP, Ealick SE Biochemistry. 2013 Sep 30. PMID:24079939 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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