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Structure paper

TitleStructures of the nitrogenase complex prepared under catalytic turnover conditions.
Journal, issue, pagesScience, Vol. 377, Issue 6608, Page 865-869, Year 2022
Publish dateAug 19, 2022
AuthorsHannah L Rutledge / Brian D Cook / Hoang P M Nguyen / Mark A Herzik / F Akif Tezcan /
PubMed AbstractThe enzyme nitrogenase couples adenosine triphosphate (ATP) hydrolysis to the multielectron reduction of atmospheric dinitrogen into ammonia. Despite extensive research, the mechanistic details of ...The enzyme nitrogenase couples adenosine triphosphate (ATP) hydrolysis to the multielectron reduction of atmospheric dinitrogen into ammonia. Despite extensive research, the mechanistic details of ATP-dependent energy transduction and dinitrogen reduction by nitrogenase are not well understood, requiring new strategies to monitor its structural dynamics during catalytic action. Here, we report cryo-electron microscopy structures of the nitrogenase complex prepared under enzymatic turnover conditions. We observe that asymmetry governs all aspects of the nitrogenase mechanism, including ATP hydrolysis, protein-protein interactions, and catalysis. Conformational changes near the catalytic iron-molybdenum cofactor are correlated with the nucleotide-hydrolysis state of the enzyme.
External linksScience / PubMed:35901182 / PubMed Central
MethodsEM (single particle)
Resolution1.91 - 3.01 Å
Structure data

26756

7ut6

EMDB-26756, PDB-7ut6:
C1 symmetric cryoEM structure of Azotobacter vinelandii MoFeP under non-turnover conditions
Method: EM (single particle) / Resolution: 1.91 Å

26757

7ut7

EMDB-26757, PDB-7ut7:
C2 symmetric cryoEM structure of Azotobacter vinelandii MoFeP under non-turnover conditions
Method: EM (single particle) / Resolution: 1.91 Å

EMDB-26758: Consensus cryoEM map of Azotobacter vinelandii MoFeP in a 1:1 complex (ATP-bound) with FeP during catalytic N2 reduction
Method: EM (single particle) / Resolution: 2.38 Å

EMDB-26759: Locally refined cryoEM map of Azotobacter vinelandii FeP in a 1:1 complex (ATP-bound) with MoFeP during catalytic N2 reduction
Method: EM (single particle) / Resolution: 2.75 Å

26760

7ut8

EMDB-26760, PDB-7ut8:
CryoEM structure of Azotobacter vinelandii nitrogenase complex (1:1 FeP:MoFeP, ATP-bound) during catalytic N2 reduction
Method: EM (single particle) / Resolution: 2.43 Å

EMDB-26761: Consensus cryoEM map of Azotobacter vinelandii MoFeP in a 1:1 complex (ADP/ATP-bound) with FeP during catalytic N2 reduction
Method: EM (single particle) / Resolution: 2.34 Å

EMDB-26762: Locally refined cryoEM map of Azotobacter vinelandii FeP in a 1:1 complex (ADP/ATP-bound) with MoFeP during catalytic N2 reduction
Method: EM (single particle) / Resolution: 3.01 Å

26763

7ut9

EMDB-26763, PDB-7ut9:
CryoEM structure of Azotobacter vinelandii nitrogenase complex (1:1 FeP:MoFeP, ADP/ATP-bound) during catalytic N2 reduction
Method: EM (single particle) / Resolution: 2.44 Å

26764

7uta

EMDB-26764, PDB-7uta:
CryoEM structure of Azotobacter vinelandii nitrogenase complex (2:1 FeP:MoFeP) inhibited by BeFx during catalytic N2 reduction
Method: EM (single particle) / Resolution: 2.4 Å

27639

8dpn

EMDB-27639, PDB-8dpn:
CryoEM structure of Azotobacter vinelandii nitrogenase MoFeP during catalytic N2 reduction
Method: EM (single particle) / Resolution: 2.49 Å

Chemicals

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

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

ChemComp-FE:
Unknown entry

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

ChemComp-HOH:
WATER

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-MG:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-0BE:
BERYLLIUM

Source
  • azotobacter vinelandii dj (bacteria)
KeywordsOXIDOREDUCTASE / nitrogenase / MoFeP / nitrogen fixation / FeP

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