9uay

Crystal structure of CmnI

spinqualitylabelsall models 9uay, resolution 2.17Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9uay is a 2 chain structure with sequence from Saccharothrix mutabilis subsp. capreolus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.17Å Ligands: AE3, AE4, PEG, PG4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Capreomycin (CMN) is a nonribosomal peptide (NRP) antituberculosis antibiotic. CMN biosynthesis involves a non-canonical trans-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(1) 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 trans-iterative A domain in the NRPS machinery. Biosynthesis of Antituberculosis Antibiotic Capreomycin Involves a trans-Iterative Adenylation Domain within the Nonribosomal Peptide Synthetase Machinery.,Lai YT, Peng CY, Liao HT, Hsiao PY, Hsieh CK, Luo YR, Huang SC, Wang YL, Ma T, Chen YR, Kuo YM, Lin YC, Chu J, Chang CY Org Lett. 2025 Aug 29;27(34):9553-9558. doi: 10.1021/acs.orglett.5c03112. Epub , 2025 Aug 15. PMID:40815678 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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