› 1yd4

X-ray diffraction
1.9Å resolution

Crystal structure of the GIY-YIG N-terminal endonuclease domain of UvrC from Thermotoga maritima: Point mutant Y29F bound to its catalytic divalent cation

Released:
DOI: 10.2210/pdb1yd4/pdb
Model geometry
Fit model/data
PDB entry 1yd4 coloured by chain, front view.
PDB entry 1yd4 coloured by chain, side view.
PDB entry 1yd4 coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Structural insights into the first incision reaction during nucleotide excision repair.
Truglio JJ, Rhau B, Croteau DL, Wang L, Skorvaga M, Karakas E, DellaVecchia MJ, Wang H, Van Houten B, Kisker C
EMBO J 24 885-94 (2005)
PMID: 15692561

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194485 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UvrABC system protein C Chain: A
Molecule details ›
Chain: A
Length: 96 amino acids
Theoretical weight: 11.36 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WYA3 (Residues: 1-96; Coverage: 17%)
Gene names: TM_0265, uvrC
Sequence domains: GIY-YIG catalytic domain
Structure domains: GIY-YIG endonuclease

Ligands and Environments

1 bound ligand:
Ligand MN 3 x MN
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: NSLS BEAMLINE X26C
Spacegroup: P43212
Unit cell:
a: 54.949Å b: 54.949Å c: 109.187Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.171 0.206
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Nucleases: diversity of structure, function and mechanism.
Yang W. (2011)
9 more