› 4at1

X-ray diffraction
2.6Å resolution

STRUCTURAL CONSEQUENCES OF EFFECTOR BINDING TO THE T STATE OF ASPARTATE CARBAMOYLTRANSFERASE. CRYSTAL STRUCTURES OF THE UNLIGATED AND ATP-, AND CTP-COMPLEXED ENZYMES AT 2.6-ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb4at1/pdb
PDB entry 4at1 coloured by chain, front view.
PDB entry 4at1 coloured by chain, side view.
PDB entry 4at1 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-A resolution.
Stevens RC, Gouaux JE, Lipscomb WN
Biochemistry 29 7691-701 (1990)
PMID: 2271528

Function and Biology Details

Reaction catalysed: 
Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141554 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Aspartate carbamoyltransferase catalytic subunit Chains: A, C
Molecule details ›
Chains: A, C
Length: 310 amino acids
Theoretical weight: 34.34 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P0A786 (Residues: 2-311; Coverage: 100%)
Gene names: JW4204, b4245, pyrB
Sequence domains:
Structure domains: Aspartate/ornithine carbamoyltransferase
Aspartate carbamoyltransferase regulatory chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 153 amino acids
Theoretical weight: 17.07 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P0A7F3 (Residues: 1-153; Coverage: 100%)
Gene names: JW4203, b4244, pyrI
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand ATP 2 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P321
Unit cell:
a: 122Å b: 122Å c: 142Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.16 0.16 not available
Expression system: Not provided

Quick links

Citations

8 review citations

The functions and consensus motifs of nine types of peptide segments that form different types of nucleotide-binding sites.
Traut TW. (1994)
7 more

5 mentions without citation

Allostery and cooperativity in Escherichia coli aspartate transcarbamoylase.
Kantrowitz ER. (2012)
4 more