› 3dj4

X-ray diffraction
2.38Å resolution

Crystal Structure of GlmU from Mycobacterium tuberculosis in complex with URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE.

Released:
DOI: 10.2210/pdb3dj4/pdb
PDB entry 3dj4 coloured by chain, front view.
PDB entry 3dj4 coloured by chain, side view.
PDB entry 3dj4 coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
PknB-mediated phosphorylation of a novel substrate, N-acetylglucosamine-1-phosphate uridyltransferase, modulates its acetyltransferase activity.
Parikh A, Verma SK, Khan S, Prakash B, Nandicoori VK
J Mol Biol 386 451-64 (2009)
PMID: 19121323

Function and Biology Details

Reactions catalysed: 
Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161813 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional protein GlmU Chain: A
Molecule details ›
Chain: A
Length: 495 amino acids
Theoretical weight: 51.64 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WMN3 (Residues: 1-495; Coverage: 100%)
Gene names: Rv1018c, glmU
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 1 x MG
Ligand CO 1 x CO
Ligand UD1 1 x UD1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: R3
Unit cell:
a: 78.6Å b: 78.6Å c: 278Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.194 0.257
Expression system: Escherichia coli

Quick links

Citations

20 review citations

Eukaryote-like serine/threonine kinases and phosphatases in bacteria.
Pereira et al. (2011)
19 more

9 mentions without citation

The structural biology of enzymes involved in natural product glycosylation.
Singh et al. (2012)
8 more