6qp3

Crystal structure of the PLP-bound C-S lyase from Bacillus subtilis (strain 168)

spinqualitylabelsall models 6qp3, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6qp3 is a 4 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: ACT, PLP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CBL_BACSU Catalyzes the transformation of cystathionine to homocysteine. Also exhibits cysteine desulfhydrase activity in vitro, producing sulfide from cysteine. Publication Abstract from PubMed Body odour is a characteristic trait of Homo sapiens, however its role in human behaviour and evolution is poorly understood. Remarkably, body odour is linked to the presence of a few species of commensal microbes. Herein we discover a bacterial enzyme, limited to odour-forming staphylococci that are able to cleave odourless precursors of thioalcohols, the most pungent components of body odour. We demonstrated using phylogenetics, biochemistry and structural biology that this cysteine-thiol lyase (C-T lyase) is a PLP-dependent enzyme that moved horizontally into a unique monophyletic group of odour-forming staphylococci about 60 million years ago, and has subsequently tailored its enzymatic function to human-derived thioalcohol precursors. Significantly, transfer of this enzyme alone to non-odour producing staphylococci confers odour production, demonstrating that this C-T lyase is both necessary and sufficient for thioalcohol formation. The structure of the C-T lyase compared to that of other related enzymes reveals how the adaptation to thioalcohol precursors has evolved through changes in the binding site to create a constrained hydrophobic pocket that is selective for branched aliphatic thioalcohol ligands. The ancestral acquisition of this enzyme, and the subsequent evolution of the specificity for thioalcohol precursors implies that body odour production in humans is an ancient process. The molecular basis of thioalcohol production in human body odour.,Rudden M, Herman R, Rose M, Bawdon D, Cox DS, Dodson E, Holden MTG, Wilkinson AJ, James AG, Thomas GH Sci Rep. 2020 Jul 27;10(1):12500. doi: 10.1038/s41598-020-68860-z. PMID:32719469 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cystathionine beta-lyase

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