› 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 4avc coloured by chain and viewed from the front.
PDB 4avc coloured by chain and viewed from the side.
PDB 4avc coloured by chain and viewed from the top.
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
OpenAccess logo 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)
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

12 review citations

Bacterial Sirtuins Overview: An Open Niche to Explore.
Gallego-Jara et al. (2021)
11 more

2 mentions without citation

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