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7tpy

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

Structural highlights

7tpy is a 1 chain structure with sequence from Azotobacter vinelandii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.48Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NIFH1_AZOVI The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein (component 2) and a component 1 which is either a molybdenum-iron protein, a vanadium-iron, or an iron-iron protein.[HAMAP-Rule:MF_00533]

Publication Abstract from PubMed

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 (CO2) reduction and facilitating MoFe protein metallocluster biosynthesis. The precise role(s) of the Fe protein Fe4S4 cluster in some of these processes remains ill-defined. Herein, we report crystallographic data demonstrating ATP-dependent chalcogenide exchange at the Fe4S4 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 Fe4S4 cluster is capable of core substitution reactions under certain conditions, adding to the Fe protein's repertoire of unique properties.

Selenocyanate derived Se-incorporation into the nitrogenase Fe protein cluster.,Buscagan TM, Kaiser JT, Rees DC Elife. 2022 Jul 29;11. pii: 79311. doi: 10.7554/eLife.79311. PMID:35904245^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Buscagan TM, Kaiser JT, Rees DC. Selenocyanate derived Se-incorporation into the nitrogenase Fe protein cluster. Elife. 2022 Jul 29;11. pii: 79311. doi: 10.7554/eLife.79311. PMID:35904245 doi:http://dx.doi.org/10.7554/eLife.79311