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Structure paper

TitleTyrosine-Coordinated P-Cluster in G. diazotrophicus Nitrogenase: Evidence for the Importance of O-Based Ligands in Conformationally Gated Electron Transfer.
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 138, Page 10124-10127, Year 2016
Publish dateJun 30, 2016 (structure data deposition date)
AuthorsOwens, C.P. / Katz, F.E. / Carter, C.H. / Oswald, V.F. / Tezcan, F.A.
External linksJ. Am. Chem. Soc. / PubMed:27487256
MethodsX-ray diffraction
Resolution1.83 - 2.592 Å
Structure data

PDB-5koh:
Nitrogenase MoFeP from Gluconacetobacter diazotrophicus in dithionite reduced state
Method: X-RAY DIFFRACTION / Resolution: 1.83 Å

PDB-5koj:
Nitrogenase MoFeP protein in the IDS oxidized state
Method: X-RAY DIFFRACTION / Resolution: 2.592 Å

Chemicals

ChemComp-HCA:
3-HYDROXY-3-CARBOXY-ADIPIC ACID

ChemComp-ICS:
iron-sulfur-molybdenum cluster with interstitial carbon

ChemComp-MRD:
(4R)-2-METHYLPENTANE-2,4-DIOL / precipitant*YM

ChemComp-CLF:
FE(8)-S(7) CLUSTER

ChemComp-FE:
Unknown entry

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

ChemComp-HOH:
WATER

Source
  • gluconacetobacter diazotrophicus (strain atcc 49037 / dsm 5601 / pal5) (bacteria)
KeywordsOXIDOREDUCTASE / Nitrogenase / electron transfer / P-cluster

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