› 4ava

X-ray diffraction
1.7Å resolution

Crystal structure of protein lysine acetyltransferase Rv0998 from Mycobacterium tuberculosis

Released:
DOI: 10.2210/pdb4ava/pdb
PDB entry 4ava coloured by chain, front view.
PDB entry 4ava coloured by chain, side view.
PDB entry 4ava 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 Chain: A
Molecule details ›
Chain: A
Length: 333 amino acids
Theoretical weight: 35.66 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

5 bound ligands:
Ligand ACO 1 x ACO
Ligand ACT 1 x ACT
Ligand EDO 4 x EDO
Ligand PEG 2 x PEG
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P212121
Unit cell:
a: 61.418Å b: 65.447Å c: 77.761Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.191 0.23
Expression system: Escherichia coli BL21

Quick links

Citations

11 review citations

Regulation of bacterial physiology by lysine acetylation of proteins.
Bernal et al. (2014)
10 more

4 mentions without citation

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