› 1f0p

X-ray diffraction
1.9Å resolution

Function and Biology Details

Reactions catalysed: 
2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-trehalose + alpha,alpha'-trehalose 6,6'-bismycolate
Acyl-CoA + 1,2-diacylglycerol = CoA + triacylglycerol
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162089 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Diacylglycerol acyltransferase/mycolyltransferase Ag85B Chain: A
Molecule details ›
Chain: A
Length: 285 amino acids
Theoretical weight: 30.68 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Mycolicibacterium smegmatis
UniProt:
  • Canonical: P9WQP1 (Residues: 41-325; Coverage: 100%)
Gene names: MTCY180.32, Rv1886c, fbpB
Sequence domains: Putative esterase
Structure domains: alpha/beta hydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
2 bound ligands:
Ligand MPD 3 x MPD
Ligand MES 1 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P3121
Unit cell:
a: 73.21Å b: 73.21Å c: 92.544Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.192 0.284
Expression system: Mycolicibacterium smegmatis

Quick links

Citations

18 review citations

Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis.
Takayama et al. (2005)
17 more

11 mentions without citation

Uptake of unnatural trehalose analogs as a reporter for Mycobacterium tuberculosis.
Backus et al. (2011)
10 more