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TitleATP binding controls the molecular function of bacterial MutS2 by mediating closure of the dimeric clamp structure.
Journal, issue, pagesStructure, Vol. 33, Page 1007-1015.e4, Year 2025
Publish dateNov 1, 2024 (structure data deposition date)
AuthorsFukui, K. / Murakawa, T. / Hino, N. / Kondo, N. / Yano, T.
External linksStructure / PubMed:40157362
MethodsX-ray diffraction
Resolution2.49 Å
Structure data

PDB-9kce:
Crystal Structure of the ATP analog-bound closed state of Thermotoga maritima MutS2
Method: X-RAY DIFFRACTION / Resolution: 2.49 Å

Chemicals

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • thermotoga maritima msb8 (bacteria)
KeywordsDNA BINDING PROTEIN / ATPase / MutS family / MutS2 / homologous recombination

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