› 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:
DOI: 10.2210/pdb4fmn/pdb
PDB 4fmn coloured by chain and viewed from the front.
PDB 4fmn coloured by chain and viewed from the side.
PDB 4fmn coloured by chain and viewed from the top.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site.
Gueneau E, Dherin C, Legrand P, Tellier-Lebegue C, Gilquin B, Bonnesoeur P, Londino F, Quemener C, Le Du MH, Márquez JA, Moutiez M, Gondry M, Boiteux S, Charbonnier JB
Nat. Struct. Mol. Biol. 20 461-8 (2013)
PMID: 23435383

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:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero 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:
Ligand GOL 5 x GOL
Ligand EDO 6 x EDO
Ligand ZN 2 x ZN
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

Quick links

Citations

11 review citations

Stochastic Processes and Component Plasticity Governing DNA Mismatch Repair.
Liu et al. (2018)
10 more

2 mentions without citation

R.I.P. to the PIP: PCNA-binding motif no longer considered specific: PIP motifs and other related sequences are not distinct entities and can bind multiple proteins involved in genome maintenance.
Boehm et al. (2016)
1 more