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Structure paper

TitleStructural and biochemical insights into the disulfide reductase mechanism of DsbD, an essential enzyme for neisserial pathogens.
Journal, issue, pagesJ. Biol. Chem., Vol. 293, Page 16559-16571, Year 2018
Publish dateJun 6, 2018 (structure data deposition date)
AuthorsSmith, R.P. / Mohanty, B. / Mowlaboccus, S. / Paxman, J.J. / Williams, M.L. / Headey, S.J. / Wang, G. / Subedi, P. / Doak, B.C. / Kahler, C.M. ...Smith, R.P. / Mohanty, B. / Mowlaboccus, S. / Paxman, J.J. / Williams, M.L. / Headey, S.J. / Wang, G. / Subedi, P. / Doak, B.C. / Kahler, C.M. / Scanlon, M.J. / Heras, B.
External linksJ. Biol. Chem. / PubMed:30181210
MethodsX-ray diffraction
Resolution1.603 - 2.556 Å
Structure data

PDB-6dnl:
Crystal Structure of Neisseria meningitidis DsbD c-terminal domain in the reduced form
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-6dnu:
Crystal Structure of Neisseria meningitidis DsbD c-terminal domain in the oxidised form
Method: X-RAY DIFFRACTION / Resolution: 2.283 Å

PDB-6dnv:
Crystal Structure of Neisseria meningitidis DsbD n-terminal domain in the reduced form
Method: X-RAY DIFFRACTION / Resolution: 1.603 Å

PDB-6dps:
Crystal Structure of Neisseria meningitidis DsbD n-terminal domain in the oxidised form
Method: X-RAY DIFFRACTION / Resolution: 2.556 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

ChemComp-P6G:
HEXAETHYLENE GLYCOL / precipitant*YM

ChemComp-SO4:
SULFATE ION

Source
  • neisseria meningitidis (bacteria)
  • neisseria meningitidis (strain alpha14) (bacteria)
KeywordsOXIDOREDUCTASE / disulphide reductase / Dsb proteins

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