3n5f | pdb_00003n5f

Crystal Structure of L-N-carbamoylase from Geobacillus stearothermophilus CECT43

spinqualitylabelsall models 3n5f, resolution 2.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3n5f is a 2 chain structure with sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.75Å Ligands: CAC, CO, IPA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AMAB2_GEOSE Publication Abstract from PubMed N-Carbamoyl-l-amino acid amidohydrolases (l-carbamoylases) are important industrial enzymes used in kinetic resolution of racemic mixtures of N-carbamoyl-amino acids due to their strict enantiospecificity. In this work, we report the first l-carbamoylase structure belonging to Geobacillus stearothermophilus CECT43 (BsLcar), at a resolution of 2.7 A. Structural analysis of BsLcar and several members of the peptidase M20/M25/M40 family confirmed the expected conserved residues at the active site in this family, and site-directed mutagenesis revealed their relevance to substrate binding. We also found an unexpectedly conserved arginine residue (Arg(234) in BsLcar), proven to be critical for dimerization of the enzyme. The mutation of this sole residue resulted in a total loss of activity and prevented the formation of the dimer in BsLcar. Comparative studies revealed that the dimerization domain of the peptidase M20/M25/M40 family is a "small-molecule binding domain," allowing further evolutionary considerations for this enzyme family. Mutational and structural analysis of L-N-carbamoylase reveals new insights into a peptidase m20/m25/m40 family member.,Martinez-Rodriguez S, Garcia-Pino A, Las Heras-Vazquez FJ, Clemente-Jimenez JM, Rodriguez-Vico F, Garcia-Ruiz JM, Loris R, Gavira JA J Bacteriol. 2012 Nov;194(21):5759-68. doi: 10.1128/JB.01056-12. Epub 2012 Aug, 17. PMID:22904279 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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