› 1hru

X-ray diffraction
2Å resolution

THE STRUCTURE OF THE YRDC GENE PRODUCT FROM E.COLI

Released:
DOI: 10.2210/pdb1hru/pdb
PDB entry 1hru coloured by chain, front view.
PDB entry 1hru coloured by chain, side view.
PDB entry 1hru coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The structure of the yrdC gene product from Escherichia coli reveals a new fold and suggests a role in RNA binding.
Teplova M, Tereshko V, Sanishvili R, Joachimiak A, Bushueva T, Anderson WF, Egli M
Protein Sci 9 2557-66 (2000)
PMID: 11206077

Function and Biology Details

Reaction catalysed: 
L-threonine + ATP + HCO(3)(-) = L-threonylcarbamoyladenylate + diphosphate + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155338 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Threonylcarbamoyl-AMP synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 188 amino acids
Theoretical weight: 20.7 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P45748 (Residues: 1-188; Coverage: 99%)
Gene names: JW3243, b3282, rimN, tsaC, yrdC
Sequence domains: Telomere recombination
Structure domains: DHBP synthase

Ligands and Environments

1 bound ligand:
Ligand PO4 2 x PO4
1 modified residue:
Ligand MSE 4 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 60.5Å b: 71.65Å c: 55.28Å
α: 90° β: 103.25° γ: 90°
R-values:
R R work R free
0.202 0.202 0.214
Expression system: Escherichia coli

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Citations

12 review citations

'Conserved hypothetical' proteins: prioritization of targets for experimental study.
Galperin et al. (2004)
11 more

10 mentions without citation

An NMR approach to structural proteomics.
Yee et al. (2002)
9 more