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Structure paper

TitleA Lynch syndrome-associated mutation at a Bergerat ATP-binding fold destabilizes the structure of the DNA mismatch repair endonuclease MutL.
Journal, issue, pagesJ. Biol. Chem., Vol. 295, Page 11643-11655, Year 2020
Publish dateFeb 19, 2020 (structure data deposition date)
AuthorsIzuhara, K. / Fukui, K. / Murakawa, T. / Baba, S. / Kumasaka, T. / Uchiyama, K. / Yano, T.
External linksJ. Biol. Chem. / PubMed:32571878
MethodsX-ray diffraction
Resolution1.69105685009 - 3.1594962224 Å
Structure data

PDB-6lzi:
Aquifex aeolicus MutL ATPase domain complexed with ADP
Method: X-RAY DIFFRACTION / Resolution: 1.69105685009 Å

PDB-6lzj:
Aquifex aeolicus MutL ATPase domain complexed with AMPPCP
Method: X-RAY DIFFRACTION / Resolution: 1.72835563454 Å

PDB-6lzk:
Aquifex aeolicus MutL ATPase domain with K252N mutation
Method: X-RAY DIFFRACTION / Resolution: 3.1594962224 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-HOH:
WATER

ChemComp-ACP:
PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / AMP-PCP, energy-carrying molecule analogue*YM

ChemComp-NA:
Unknown entry

Source
  • aquifex aeolicus (strain vf5) (bacteria)
  • aquifex aeolicus vf5 (bacteria)
KeywordsDNA BINDING PROTEIN / DNA repair / ATPase

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