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TitleThe Structure of Clostridioides difficile SecA2 ATPase Exposes Regions Responsible for Differential Target Recognition of the SecA1 and SecA2-Dependent Systems.
Journal, issue, pagesInt J Mol Sci, Vol. 21, Year 2020
Publish dateOct 14, 2019 (structure data deposition date)
AuthorsLindic, N. / Loboda, J. / Usenik, A. / Vidmar, R. / Turk, D.
External linksInt J Mol Sci / PubMed:32858965
MethodsX-ray diffraction
Resolution2.9 Å
Structure data

PDB-6t4h:
Crystal structure of the accessory translocation ATPase, SecA2, from Clostridium difficile, in complex with adenosine-5'-(gamma-thio)-triphosphate
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

Chemicals

ChemComp-AGS:
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogue*YM

ChemComp-HOH:
WATER

Source
  • peptoclostridium difficile (strain 630) (bacteria)
KeywordsPROTEIN TRANSPORT / SecA2 / ATPase / Pathogenesis

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