6q71

Crystal structure of the alanine racemase Bsu17640 from Bacillus subtilis in the presence of Bis-Tris propane

spinqualitylabelsall models 6q71, resolution 1.92Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6q71 is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.92Å Ligands: CL, MG, PLP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ALR2_BACSU Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. Publication Abstract from PubMed Pyridoxal 5'-phosphate (PLP) is a versatile cofactor involved in a large variety of enzymatic processes. Most of PLP-catalysed reactions, such as those of alanine racemases (AlaRs), present a common resting state in which the PLP is covalently bound to an active-site lysine to form an internal aldimine. The crystal structure of BsAlaR grown in the presence of Tris lacks this covalent linkage and the PLP cofactor appears deformylated. However, loss of activity in a Tris buffer only occurred after the solution was frozen prior to carrying out the enzymatic assay. This evidence strongly suggests that Tris can access the active site at subzero temperatures and behave as an alternate racemase substrate leading to mechanism-based enzyme inactivation, a hypothesis that is supported by additional X-ray structures and theoretical results from QM/MM calculations. Taken together, our findings highlight a possibly underappreciated role for a common buffer component widely used in biochemical and biophysical experiments. Cold-induced aldimine bond cleavage by Tris in Bacillus subtilis alanine racemase.,Bernardo-Garcia N, Sanchez-Murcia PA, Espaillat A, Martinez-Caballero S, Cava F, Hermoso JA, Gago F Org Biomol Chem. 2019 Apr 12. doi: 10.1039/c9ob00223e. PMID:30977502 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Alanine racemase 3D structures

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