4fmn

X-ray diffraction
2.69Å resolution

Structure of the C-terminal domain of the Saccharomyces cerevisiae MUTL alpha (MLH1/PMS1) heterodimer bound to a fragment of NTG2

Released:

Function and Biology Details

Reaction catalysed:
The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
Non-polymer only trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
DNA mismatch repair protein MLH1 Chain: A
Molecule details ›
Chain: A
Length: 288 amino acids
Theoretical weight: 33.24 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P38920 (Residues: 485-769; Coverage: 37%)
Gene names: MLH1, PMS2, YM8520.16, YMR167W
Sequence domains: DNA mismatch repair protein Mlh1 C-terminus
DNA mismatch repair protein PMS1 Chain: B
Molecule details ›
Chain: B
Length: 240 amino acids
Theoretical weight: 27.95 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P14242 (Residues: 635-873; Coverage: 27%)
Gene names: N2317, PMS1, YNL082W
Sequence domains: MutL C terminal dimerisation domain
Endonuclease III homolog 2 Chain: C
Molecule details ›
Chain: C
Length: 9 amino acids
Theoretical weight: 1.09 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Not provided
UniProt:
  • Canonical: Q08214 (Residues: 22-29; Coverage: 2%)
Gene names: NTG2, SCR2, YOL043C

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: C2
Unit cell:
a: 190.94Å b: 66.3Å c: 74.11Å
α: 90° β: 90.15° γ: 90°
R-values:
R R work R free
0.17 0.169 0.192
Expression systems:
  • Escherichia coli
  • Not provided