› 2gej

X-ray diffraction
2.6Å resolution

Crystal Structure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP-Man

Released:
DOI: 10.2210/pdb2gej/pdb
PDB 2gej coloured by chain and viewed from the front.
PDB 2gej coloured by chain and viewed from the side.
PDB 2gej coloured by chain and viewed from the top.
Source organism: Mycolicibacterium smegmatis MC2 155
Primary publication:
Molecular recognition and interfacial catalysis by the essential phosphatidylinositol mannosyltransferase PimA from mycobacteria.
Guerin ME, Kordulakova J, Schaeffer F, Svetlikova Z, Buschiazzo A, Giganti D, Gicquel B, Mikusova K, Jackson M, Alzari PM
J. Biol. Chem. 282 20705-14 (2007)
PMID: 17510062

Function and Biology Details

Reaction catalysed: 
GDP-alpha-D-mannose + 1-phosphatidyl-1D-myo-inositol = GDP + 2-O-(alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
Biochemical function:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphatidyl-myo-inositol mannosyltransferase Chain: A
Molecule details ›
Chain: A
Length: 406 amino acids
Theoretical weight: 43.44 KDa
Source organism: Mycolicibacterium smegmatis MC2 155
Expression system: Escherichia coli
UniProt:
  • Canonical: A0QWG6 (Residues: 1-386; Coverage: 100%)
Gene names: MSMEG_2935, MSMEI_2861, pimA
Sequence domains:
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments

1 bound ligand:
Ligand GDD 1 x GDD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 37.071Å b: 72.747Å c: 137.166Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.192 0.245
Expression system: Escherichia coli

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Citations

18 review citations

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

17 mentions without citation

3D Structure and Function of Glycosyltransferases Involved in N-glycan Maturation.
Nagae et al. (2020)
16 more