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Structure paper

TitleStructural basis for HOCl recognition and regulation mechanisms of HypT, a hypochlorite-specific transcriptional regulator.
Journal, issue, pagesProc. Natl. Acad. Sci. U.S.A., Vol. 116, Page 3740-3745, Year 2019
Publish dateSep 13, 2017 (structure data deposition date)
AuthorsJo, I. / Kim, D. / No, T. / Hong, S. / Ahn, J. / Ryu, S. / Ha, N.C.
External linksProc. Natl. Acad. Sci. U.S.A. / PubMed:30733296
MethodsX-ray diffraction
Resolution1.752 - 3.3 Å
Structure data

PDB-5ydo:
Regulatory domain of HypT from Salmonella typhimurium (apo-form)
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-5ydv:
Regulatory domain of HypT from Salmonella typhimurium complexed with HOCl (HOCl-bound form)
Method: X-RAY DIFFRACTION / Resolution: 1.752 Å

PDB-5ydw:
Full-length structure of HypT from Salmonella typhimuriuma (hypochlorite-specific LysR-type transcriptional regulator)
Method: X-RAY DIFFRACTION / Resolution: 3.3 Å

PDB-5yer:
Regulatory domain of HypT from Salmonella typhimurium (Bromide ion-bound)
Method: X-RAY DIFFRACTION / Resolution: 2.301 Å

PDB-5yez:
Regulatory domain of HypT M206Q mutant from Salmonella typhimurium
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-8TR:
hypochlorous acid

ChemComp-BR:
BROMIDE ION

Source
  • salmonella choleraesuis (bacteria)
  • salmonella typhimurium (bacteria)
KeywordsDNA BINDING PROTEIN / HOCl / HOCl-specific transcription factor / LysR-type transcription regulator / Hypochlorous acid / hypochlorite / regulatory domain / HypT

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