Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen IH, Cheng T, Wang YL, Huang SJ, Hsiao YH, Lai YT, Toh SI, Chu J, Rudolf JD, Chang CY. Characterization and Structural Determination of CmnG-A, the Adenylation Domain That Activates the Nonproteinogenic Amino Acid Capreomycidine in Capreomycin Biosynthesis. Chembiochem. 2022 Dec 16;23(24):e202200563. PMID:36278314 doi:10.1002/cbic.202200563
