› 2yqc

X-ray diffraction
1.9Å resolution

Crystal Structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase from Candida albicans, in the apo-like form

Released:
DOI: 10.2210/pdb2yqc/pdb
PDB entry 2yqc coloured by chain, front view.
PDB entry 2yqc coloured by chain, side view.
PDB entry 2yqc coloured by chain, top view.
Source organism: Candida albicans
Primary publication:
Crystal structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase from Candida albicans and catalytic reaction mechanism.
Maruyama D, Nishitani Y, Nonaka T, Kita A, Fukami TA, Mio T, Yamada-Okabe H, Yamada-Okabe T, Miki K
J Biol Chem 282 17221-30 (2007)
PMID: 17392279

Function and Biology Details

Reaction catalysed: 
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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130802 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylglucosamine pyrophosphorylase Chain: A
Molecule details ›
Chain: A
Length: 486 amino acids
Theoretical weight: 54.73 KDa
Source organism: Candida albicans
Expression system: Escherichia coli
UniProt:
  • Canonical: O74933 (Residues: 1-486; Coverage: 100%)
Gene name: UAP1
Sequence domains: UTP--glucose-1-phosphate uridylyltransferase
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P21
Unit cell:
a: 47.774Å b: 62.891Å c: 90.602Å
α: 90° β: 97.82° γ: 90°
R-values:
R R work R free
0.174 0.174 0.201
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Cytoplasmic steps of peptidoglycan biosynthesis.
Barreteau et al. (2008)
6 more

3 mentions without citation

Crystal structure of PG16 and chimeric dissection with somatically related PG9: structure-function analysis of two quaternary-specific antibodies that effectively neutralize HIV-1.
Pancera et al. (2010)
2 more