› 2j8r

X-ray diffraction
1.55Å resolution

Structure of P. aeruginosa acetyltransferase PA4866 solved in complex with L-Methionine sulfoximine

Released:
DOI: 10.2210/pdb2j8r/pdb
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Source organism: Pseudomonas aeruginosa
Primary publication:
l-Methionine sulfoximine, but not phosphinothricin, is a substrate for an acetyltransferase (gene PA4866) from Pseudomonas aeruginosa: structural and functional studies.
Davies AM, Tata R, Beavil RL, Sutton BJ, Brown PR
Biochemistry 46 1829-39 (2007)
PMID: 17253769

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190982 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-methionine sulfoximine/L-methionine sulfone acetyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 172 amino acids
Theoretical weight: 18.73 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9HUU7 (Residues: 1-172; Coverage: 100%)
Gene names: PA4866, pitA
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments

3 bound ligands:
Ligand GOL 2 x GOL
Ligand AZI 4 x AZI
Ligand MSL 2 x MSL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: P212121
Unit cell:
a: 47.637Å b: 57.197Å c: 125.18Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.18 0.213
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress.
Hentchel et al. (2015)
1 more

3 mentions without citation

In Salmonella enterica, the Gcn5-related acetyltransferase MddA (formerly YncA) acetylates methionine sulfoximine and methionine sulfone, blocking their toxic effects.
Hentchel et al. (2015)
2 more

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