› 7r9x

X-ray diffraction
2.14Å resolution

Crystal structure of a dehydrating condensation domain, AmbE-CmodAA, involved in nonribosomal peptide synthesis

Released:
DOI: 10.2210/pdb7r9x/pdb
PDB entry 7r9x coloured by chain, front view.
PDB entry 7r9x coloured by chain, side view.
PDB entry 7r9x coloured by chain, top view.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
Structure and Function of a Dehydrating Condensation Domain in Nonribosomal Peptide Biosynthesis.
Patteson JB, Fortinez CM, Putz AT, Rodriguez-Rivas J, Bryant LH, Adhikari K, Weigt M, Schmeing TM, Li B
J Am Chem Soc (2022)
PMID: 35895935

Function and Biology Details

Reaction catalysed: 
(1a) ATP + L-glutamate = diphosphate + (L-glutamyl)adenylate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191267 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AMB antimetabolite synthase AmbE Chains: A, B
Molecule details ›
Chains: A, B
Length: 438 amino acids
Theoretical weight: 47.99 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9I1H3 (Residues: 1353-1787; Coverage: 21%)
Gene names: PA2302, ambE
Sequence domains: Condensation domain

Ligands and Environments

2 bound ligands:
Ligand IOD 5 x IOD
Ligand NA 12 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Unit cell:
a: 89.94Å b: 106.87Å c: 108.909Å
α: 90° β: 96.252° γ: 90°
R-values:
R R work R free
0.191 0.19 0.232
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Thiamyxins: Structure and Biosynthesis of Myxobacterial RNA-Virus Inhibitors.
Haack et al. (2022)
3 more

1 mention without citation

Structural advances toward understanding the catalytic activity and conformational dynamics of modular nonribosomal peptide synthetases.
Patel et al. (2023)