› 3p32

X-ray diffraction
1.9Å resolution

Hydrolysis of GTP to GDP by an MCM-associated and MeaB- and MMAA-like G-protein from Mycobacterium tuberculosis

Released:
DOI: 10.2210/pdb3p32/pdb
PDB entry 3p32 coloured by chain, front view.
PDB entry 3p32 coloured by chain, side view.
PDB entry 3p32 coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Crystal structures of Mycobacterial MeaB and MMAA-like GTPases.
Edwards TE, Baugh L, Bullen J, Baydo RO, Witte P, Thompkins K, Phan IQ, Abendroth J, Clifton MC, Sankaran B, Van Voorhis WC, Myler PJ, Staker BL, Grundner C, Lorimer DD
J Struct Funct Genomics 16 91-9 (2015)
PMID: 25832174

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162031 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable GTPase Rv1496 Chain: A
Molecule details ›
Chain: A
Length: 355 amino acids
Theoretical weight: 38.6 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WPZ1 (Residues: 3-336; Coverage: 99%)
Gene names: MTCY277.18, Rv1496
Sequence domains: Methylmalonyl Co-A mutase-associated GTPase MeaB
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand GDP 1 x GDP
Ligand PGE 2 x PGE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: C2221
Unit cell:
a: 65.86Å b: 188.22Å c: 66.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.199 0.223
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Metallochaperones and metalloregulation in bacteria.
Capdevila et al. (2017)
1 more

3 mentions without citation

An integrated linkage, chromosome, and genome map for the yellow fever mosquito Aedes aegypti.
Timoshevskiy et al. (2013)
2 more