ISDA: 9UAY

Deposition Date 2025-04-01

Release Date 2026-03-11

Last Version Date 2026-03-11

Entry Detail

PDB ID:

9UAY

Keywords:

TRANSFERASE

Title:

Crystal structure of CmnI

Biological Source:

Source Organism(s):

Saccharothrix mutabilis subsp. capreolus (Taxon ID: 66854)

Expression System(s):

Escherichia coli bl21(de3)

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

2.17 Å

R-Value Free:

0.24

R-Value Work:

0.21

R-Value Observed:

0.21

Space Group:

C 1 2 1

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Macromolecular Entities

Structures with similar UniProt ID

Protein Blast

Polymer Type:polypeptide(L)
Molecule:CmnI
Chain IDs:A, B
Chain Length:568
Number of Molecules:2
Biological Source:Saccharothrix mutabilis subsp. capreolus

UniProt ID:A6YEI0

Ligand Molecules

AE3

AE4

PEG

PG4

Primary Citation

Biosynthesis of Antituberculosis Antibiotic Capreomycin Involves a trans -Iterative Adenylation Domain within the Nonribosomal Peptide Synthetase Machinery.

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.Show

Org. Lett. 27 9553 9558 (2025)

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

Abstact

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.

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Primary Citation of related structures

Abstact

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