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TitleComparative Sequence, Structure and Redox Analyses of Klebsiella pneumoniae DsbA Show That Anti-Virulence Target DsbA Enzymes Fall into Distinct Classes.
Journal, issue, pagesPlos One, Vol. 8, Page e80210-e80210, Year 2013
Publish dateAug 3, 2013 (structure data deposition date)
AuthorsKurth, F. / Rimmer, K. / Premkumar, L. / Mohanty, B. / Duprez, W. / Halili, M.A. / Shouldice, S.R. / Heras, B. / Fairlie, D.P. / Scanlon, M.J. / Martin, J.L.
External linksPlos One / PubMed:24244651
MethodsNMR (solution) / X-ray diffraction
Resolution1.99 Å
Structure data

PDB-2mbs:
NMR solution structure of oxidized KpDsbA
Method: SOLUTION NMR

PDB-4mcu:
Crystal structure of disulfide oxidoreductase from Klebsiella pneumoniae in reduced state
Method: X-RAY DIFFRACTION / Resolution: 1.99 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • klebsiella pneumoniae (bacteria)
KeywordsOXIDOREDUCTASE / thioredoxin domain / oxidative folding / virulence factor maturation / Thioredoxin fold / DsbA / disulfide oxidase / DsbB / Periplasmic

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