› 4avc

X-ray diffraction
2.81Å resolution

Crystal structure of protein lysine acetyltransferase Rv0998 in complex with acetyl CoA and cAMP

Released:
DOI: 10.2210/pdb4avc/pdb
PDB entry 4avc coloured by chain, front view.
PDB entry 4avc coloured by chain, side view.
PDB entry 4avc coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Cyclic AMP regulation of protein lysine acetylation in Mycobacterium tuberculosis.
Lee HJ, Lang PT, Fortune SM, Sassetti CM, Alber T
Nat Struct Mol Biol 19 811-8 (2012)
PMID: 22773105

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126489 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetyltransferase Pat Chains: A, B
Molecule details ›
Chains: A, B
Length: 333 amino acids
Theoretical weight: 36.22 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O05581 (Residues: 1-333; Coverage: 100%)
Gene name: Rv0998
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand CMP 2 x CMP
Ligand ACO 2 x ACO
Ligand PEG 3 x PEG
Ligand EDO 1 x EDO
1 modified residue:
Ligand MSE 24 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P21
Unit cell:
a: 68.661Å b: 50.151Å c: 110.102Å
α: 90° β: 106.63° γ: 90°
R-values:
R R work R free
0.202 0.198 0.267
Expression system: Escherichia coli BL21

Quick links

Citations

11 review citations

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

4 mentions without citation

Bacterial GCN5-Related N-Acetyltransferases: From Resistance to Regulation.
Favrot et al. (2016)
3 more