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TitleStructures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes.
Journal, issue, pagesIucrj, Vol. 7, Page 557-565, Year 2020
Publish dateNov 13, 2019 (structure data deposition date)
AuthorsSasaki, D. / Watanabe, T.F. / Eady, R.R. / Garratt, R.C. / Antonyuk, S.V. / Hasnain, S.S.
External linksIucrj / PubMed:32431838
MethodsX-ray diffraction
Resolution2.05 - 2.25 Å
Structure data

PDB-6tfd:
Crystal structure of nitrite and NO bound three-domain copper-containing nitrite reductase from Hyphomicrobium denitrificans strain 1NES1
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

PDB-6tfo:
Crystal structure of as isolated three-domain copper-containing nitrite reductase from Hyphomicrobium denitrificans strain 1NES1
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

Chemicals

ChemComp-CU:
COPPER (II) ION

ChemComp-NO2:
NITRITE ION

ChemComp-NO:
NITRIC OXIDE

ChemComp-HOH:
WATER

Source
  • hyphomicrobium denitrificans 1nes1 (bacteria)
KeywordsOXIDOREDUCTASE / Copper-containing nitrite reductase / Hyphomicrobium denitrificans strain 1NES1 / electron transfer

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