› 5lhu

X-ray diffraction
2.02Å resolution

ATP Phosphoribosyltransferase from Mycobacterium tuberculosis in complex with the allosteric inhibitor L-Histidine

Released:
DOI: 10.2210/pdb5lhu/pdb
PDB entry 5lhu coloured by chain, front view.
PDB entry 5lhu coloured by chain, side view.
PDB entry 5lhu coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Uncoupling conformational states from activity in an allosteric enzyme.
Pisco JP, de Chiara C, Pacholarz KJ, Garza-Garcia A, Ogrodowicz RW, Walker PA, Barran PE, Smerdon SJ, de Carvalho LPS
Nat Commun 8 203 (2017)
PMID: 28781362

Function and Biology Details

Reaction catalysed: 
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161812 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP phosphoribosyltransferase Chain: A
Molecule details ›
Chain: A
Length: 294 amino acids
Theoretical weight: 31.69 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WMN1 (Residues: 1-284; Coverage: 100%)
Gene names: MTCY261.17c, Rv2121c, hisG
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand HIS 1 x HIS
Ligand SO4 6 x SO4
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: R32
Unit cell:
a: 117.012Å b: 117.012Å c: 127.332Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.194 0.234
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Phosphoribosyltransferases and Their Roles in Plant Development and Abiotic Stress Response.
Liu et al. (2023)
6 other articles

3 mentions without citation

Insight into de-regulation of amino acid feedback inhibition: a focus on structure analysis method.
Naz et al. (2023)
2 more