› 5e38

X-ray diffraction
3Å resolution

Structural basis of mapping the spontaneous mutations with 5-flourouracil in uracil phosphoribosyltransferase from Mycobacterium tuberculosis

Released:
DOI: 10.2210/pdb5e38/pdb
PDB entry 5e38 coloured by chain, front view.
PDB entry 5e38 coloured by chain, side view.
PDB entry 5e38 coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Structural basis of mapping the spontaneous mutations with 5-flurouracil in uracil phosphoribosyltransferase from Mycobacterium tuberculosis.
Ghode P, Jobichen C, Ramachandran S, Bifani P, Sivaraman J
Biochem Biophys Res Commun 467 577-82 (2015)
PMID: 26456658

Function and Biology Details

Reaction catalysed: 
UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161408 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uracil phosphoribosyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 216 amino acids
Theoretical weight: 22.66 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WFF3 (Residues: 2-207; Coverage: 100%)
Gene names: MTV016.08c, Rv3309c, upp
Sequence domains: Uracil phosphoribosyltransferase
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P32
Unit cell:
a: 118.089Å b: 118.089Å c: 77.812Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.211 0.205 0.265
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Phosphoribosyl Diphosphate (PRPP): Biosynthesis, Enzymology, Utilization, and Metabolic Significance.
Hove-Jensen et al. (2017)
1 other article

1 mention without citation

Protein-Ligand Interactions in Scarcity: The Stringent Response from Bacteria to Metazoa, and the Unanswered Questions.
Barik S. (2023)