9S3L
ClxA from Clostridium cavendishii (apo)
Summary for 9S3L
| Entry DOI | 10.2210/pdb9s3l/pdb |
| Descriptor | Phenylacetate-CoA ligase, ZINC ION, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | atp, amide, ligase, closoxazole |
| Biological source | Clostridium cavendishii |
| Total number of polymer chains | 4 |
| Total formula weight | 180694.05 |
| Authors | Ascham, A.,Grogan, G. (deposition date: 2025-07-24, release date: 2025-11-19, Last modification date: 2025-12-10) |
| Primary citation | Ascham, A.,Tang, Q.,Fairlamb, I.J.S.,Grogan, G. Biocatalytic synthesis of phenyl benzoate esters using the amide ligase ClxA. Rsc Chem Biol, 6:1879-1884, 2025 Cited by PubMed Abstract: 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 , 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 Å 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. PubMed: 41098411DOI: 10.1039/d5cb00205b PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.57 Å) |
Structure validation
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