7XBU
Crystal structure of the adenylation domain of CmnG in complex with capreomycidine
Summary for 7XBU
| Entry DOI | 10.2210/pdb7xbu/pdb |
| Descriptor | CmnG, (2S)-amino[(4R)-2-amino-1,4,5,6-tetrahydropyrimidin-4-yl]ethanoic acid (3 entities in total) |
| Functional Keywords | adenylation, biosynthetic protein |
| Biological source | Saccharothrix mutabilis subsp. capreolus |
| Total number of polymer chains | 1 |
| Total formula weight | 56414.56 |
| 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: 36278314DOI: 10.1002/cbic.202200563 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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