7XBV

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

7XBV の概要

• エントリーDOI: 10.2210/pdb7xbv/pdb
• 分子名称: CmnG, DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: adenylation, biosynthetic protein
• 由来する生物種: Saccharothrix mutabilis subsp. capreolus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 56842.55

構造登録者

Chen, I.H.,Wang, Y.L.,Chang, C.Y. (登録日: 2022-03-22, 公開日: 2023-03-01, 最終更新日: 2023-11-29)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (1.94 Å)