9s3l | pdb_00009s3l

ClxA from Clostridium cavendishii (apo)

spinqualitylabelsall models 9s3l, resolution 2.57Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9s3l is a 4 chain structure with sequence from Clostridium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.57Å Ligands: MG, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1M6IZB6_9CLOT Publication Abstract from PubMed The synthesis of ester bonds using lipases is one of the most frequently performed reactions in biocatalysis, yet examples of the enzymatic synthesis of phenyl benzoate esters are comparatively rare. In this report we show that the ligase ClxA, from Clostridium cavendishii, initially reported to have roles in amide bond formation in the biosynthesis of benzoxazole antibiotics, is an effective catalyst for the formation of phenyl benzoate esters from acid and phenol substrates using ATP in an aqueous medium. The structure of ClxA in a complex with both AMP and 3,4-aminohydroxybenzoic acid was determined by X-ray crystallography to 2.15 A resolution and used as a platform to engineer the enzyme to create variants N226L and K140A possessing broader substrate specificity for ester formation, and also the ability to enable the synthesis of native amide product oligomers. Biocatalytic synthesis of phenyl benzoate esters using the amide ligase ClxA.,Ascham A, Tang Q, Fairlamb IJS, Grogan G RSC Chem Biol. 2025 Oct 8. doi: 10.1039/d5cb00205b. PMID:41098411 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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