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7TPY

Selenium-free nitrogenase Fe protein (Av2) from A. vinelandii (nucleotide control)

Summary for 7TPY
Entry DOI10.2210/pdb7tpy/pdb
DescriptorNitrogenase iron protein 1, IRON/SULFUR CLUSTER, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
Functional Keywordsnitrogenase, metalloprotein, iron sulfur cluster, oxidoreductase
Biological sourceAzotobacter vinelandii
Total number of polymer chains1
Total formula weight32351.39
Authors
Buscagan, T.M.,Kaiser, J.T.,Rees, D.C. (deposition date: 2022-01-26, release date: 2022-09-14, Last modification date: 2023-10-18)
Primary citationBuscagan, T.M.,Kaiser, J.T.,Rees, D.C.
Selenocyanate derived Se-incorporation into the Nitrogenase Fe protein cluster.
Elife, 11:-, 2022
Cited by
PubMed Abstract: The nitrogenase Fe protein mediates ATP-dependent electron transfer to the nitrogenase MoFe protein during nitrogen fixation, in addition to catalyzing MoFe protein-independent substrate (CO) reduction and facilitating MoFe protein metallocluster biosynthesis. The precise role(s) of the Fe protein FeS cluster in some of these processes remains ill-defined. Herein, we report crystallographic data demonstrating ATP-dependent chalcogenide exchange at the FeS cluster of the nitrogenase Fe protein when potassium selenocyanate is used as the selenium source, an unexpected result as the Fe protein cluster is not traditionally perceived as a site of substrate binding within nitrogenase. The observed chalcogenide exchange illustrates that this FeS cluster is capable of core substitution reactions under certain conditions, adding to the Fe protein's repertoire of unique properties.
PubMed: 35904245
DOI: 10.7554/eLife.79311
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.48 Å)
Structure validation

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