7XBT

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

Summary for 7XBT

Entry DOI	10.2210/pdb7xbt/pdb
Descriptor	CmnG, ADENOSINE MONOPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
Functional Keywords	adenylation, biosynthetic protein
Biological source	Saccharothrix mutabilis subsp. capreolus
Total number of polymer chains	1
Total formula weight	56613.90
Authors	Chen, I.H.,Wang, Y.L.,Chang, C.Y. (deposition date: 2022-03-22, release date: 2023-03-01, Last modification date: 2023-11-29)
Primary citation	Chen, I.H.,Cheng, T.,Wang, Y.L.,Huang, S.J.,Hsiao, Y.H.,Lai, Y.T.,Toh, S.I.,Chu, J.,Rudolf, J.D.,Chang, C.Y. Characterization and Structural Determination of CmnG-A, the Adenylation Domain That Activates the Nonproteinogenic Amino Acid Capreomycidine in Capreomycin Biosynthesis. Chembiochem, 23:e202200563-e202200563, 2022 Cited by PubMed Abstract: 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. PubMed: 36278314 DOI: 10.1002/cbic.202200563 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.84 Å)

Structure validation