7xbt

Crystal structure of the adenylation domain of CmnG in complex with AMP

spinqualitylabelsall models 7xbt, resolution 1.84Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7xbt is a 1 chain structure with sequence from Saccharothrix mutabilis subsp. capreolus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.84Å Ligands: AMP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A6YEH8_STRMP Publication Abstract from PubMed Capreomycidine (Cap) is a nonproteinogenic amino acid and building block of nonribosomal peptide (NRP) natural products. We report the formation and activation of Cap in capreomycin biosynthesis. CmnC and CmnD catalyzed hydroxylation and cyclization, respectively, of l-Arg to form l-Cap. l-Cap is then adenylated by CmnG-A before being incorporated into the nonribosomal peptide. The co-crystal structures of CmnG-A with l-Cap and adenosine nucleotides provide insights into the specificity and engineering opportunities of this unique adenylation domain. Characterization and Structural Determination of CmnG-A, the Adenylation Domain That Activates the Nonproteinogenic Amino Acid Capreomycidine in Capreomycin Biosynthesis.,Chen IH, Cheng T, Wang YL, Huang SJ, Hsiao YH, Lai YT, Toh SI, Chu J, Rudolf JD, Chang CY Chembiochem. 2022 Dec 16;23(24):e202200563. doi: 10.1002/cbic.202200563. Epub , 2022 Nov 16. PMID:36278314 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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