› 2wgs

X-ray diffraction
2.55Å resolution

Crystal structure of Mycobacterium Tuberculosis Glutamine Synthetase in complex with a purine analogue inhibitor.

Released:
DOI: 10.2210/pdb2wgs/pdb
PDB entry 2wgs coloured by chain, front view.
PDB entry 2wgs coloured by chain, side view.
PDB entry 2wgs coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Structural basis for the inhibition of Mycobacterium tuberculosis glutamine synthetase by novel ATP-competitive inhibitors.
Nilsson MT, Krajewski WW, Yellagunda S, Prabhumurthy S, Chamarahally GN, Siddamadappa C, Srinivasa BR, Yahiaoui S, Larhed M, Karlén A, Jones TA, Mowbray SL
J Mol Biol 393 504-13 (2009)
PMID: 19695264

Function and Biology Details

Reaction catalysed: 
ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dodecamer
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161831 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamine synthetase Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 486 amino acids
Theoretical weight: 54.58 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WN39 (Residues: 2-478; Coverage: 100%)
Gene names: MTCY190.31, MTCY427.01, Rv2220, glnA, glnA1
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand 1AZ 12 x 1AZ
Ligand CL 12 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 134.95Å b: 203.18Å c: 230.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.23 0.246
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Nitrogen metabolism in Mycobacterium tuberculosis physiology and virulence.
Gouzy et al. (2014)
3 more

4 mentions without citation

AMPylation: Something Old is New Again.
Woolery et al. (2010)
3 more