9UAY

Crystal structure of CmnI

Summary for 9UAY

• Entry DOI: 10.2210/pdb9uay/pdb
• Descriptor: CmnI, 3,6,9,12,15-PENTAOXAHEPTADECAN-1-OL, DI(HYDROXYETHYL)ETHER, ... (6 entities in total)
• Functional Keywords: transferase
• Biological source: Saccharothrix mutabilis subsp. capreolus
• Total number of polymer chains: 2
• Total formula weight: 124528.79

Authors

Hsiao, P.Y.,Chang, C.Y.,Peng, C.Y. (deposition date: 2025-04-01, release date: 2026-03-11)

Primary citation

Lai, Y.T.,Peng, C.Y.,Liao, H.T.,Hsiao, P.Y.,Hsieh, C.K.,Luo, Y.R.,Huang, S.C.,Wang, Y.L.,Ma, T.,Chen, Y.R.,Kuo, Y.M.,Lin, Y.C.,Chu, J.,Chang, C.Y.
Biosynthesis of Antituberculosis Antibiotic Capreomycin Involves a trans -Iterative Adenylation Domain within the Nonribosomal Peptide Synthetase Machinery.
Org.Lett., 27:9553-9558, 2025

PubMed Abstract: Capreomycin (CMN) is a nonribosomal peptide (NRP) antituberculosis antibiotic. CMN biosynthesis involves a non-canonical -iterative adenylation (A) domain. Here, we report that the A domain-less nonribosomal peptide synthetase (NRPS) module CmnI utilizes another module's A domain CmnA-A to load the required amino acid onto its thiolation (T) domain. This study provides evidence of an unusual mode of NRP biosynthesis in bacteria, involving a -iterative A domain in the NRPS machinery.

PubMed: 40815678
DOI: 10.1021/acs.orglett.5c03112

Experimental method

X-RAY DIFFRACTION (2.17 Å)