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TitleMycobacterial and Human Nitrobindins: Structure and Function.
Journal, issue, pagesAntioxid. Redox Signal., Vol. 33, Page 229-246, Year 2020
Publish dateMar 21, 2019 (structure data deposition date)
AuthorsDe Simone, G. / di Masi, A. / Vita, G.M. / Polticelli, F. / Pesce, A. / Nardini, M. / Bolognesi, M. / Ciaccio, C. / Coletta, M. / Turilli, E.S. ...De Simone, G. / di Masi, A. / Vita, G.M. / Polticelli, F. / Pesce, A. / Nardini, M. / Bolognesi, M. / Ciaccio, C. / Coletta, M. / Turilli, E.S. / Fasano, M. / Tognaccini, L. / Smulevich, G. / Abbruzzetti, S. / Viappiani, C. / Bruno, S. / Ascenzi, P.
External linksAntioxid. Redox Signal. / PubMed:32295384
MethodsX-ray diffraction
Resolution1.2 - 1.6 Å
Structure data

PDB-6r3w:
M.tuberculosis nitrobindin with a water molecule coordinated to the heme iron atom
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

PDB-6r3y:
M.tuberculosis nitrobindin with a cyanide molecule coordinated to the heme iron atom
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-HOH:
WATER

ChemComp-CYN:
CYANIDE ION

Source
  • mycobacterium tuberculosis (bacteria)
KeywordsPROTEIN BINDING / heme-protein / beta-barrel / peroxynitrite detossification / hemeproteins / peroxynitrite detoxification

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