› 6h5a

X-ray diffraction
1.88Å resolution

Crystal structure of Mycobacterium tuberculosis phosphatidylinositol phosphate synthase (PgsA1) in complex with manganese and citrate

Released:
DOI: 10.2210/pdb6h5a/pdb
PDB entry 6h5a coloured by chain, front view.
PDB entry 6h5a coloured by chain, side view.
PDB entry 6h5a coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Structure of Mycobacterium tuberculosis phosphatidylinositol phosphate synthase reveals mechanism of substrate binding and metal catalysis.
Grāve K, Bennett MD, Högbom M
Commun Biol 2 175 (2019)
PMID: 31098408

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161980 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphatidylinositol phosphate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 223 amino acids
Theoretical weight: 24.07 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WPG7 (Residues: 1-217; Coverage: 100%)
Gene names: Rv2612c, pgsA, pgsA1
Sequence domains: CDP-alcohol phosphatidyltransferase

Ligands and Environments

6 bound ligands:
Ligand MN 7 x MN
Ligand FLC 3 x FLC
Ligand OLC 3 x OLC
Ligand LFA 4 x LFA
Ligand SO4 1 x SO4
Ligand 1PE 2 x 1PE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 68.067Å b: 77.941Å c: 100.823Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.204 0.23
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Antibiotics and resistance: the two-sided coin of the mycobacterial cell wall.
Batt et al. (2020)
1 more

1 mention without citation

Structural and Functional Characterization of Phosphatidylinositol-Phosphate Biosynthesis in Mycobacteria.
Belcher Dufrisne et al. (2020)