7TPV
Selenium-free nitrogenase Fe protein (Av2) from A. vinelandii (5mM KSeCN Soaked)
Summary for 7TPV
| Entry DOI | 10.2210/pdb7tpv/pdb |
| Descriptor | Nitrogenase iron protein 1, ADENOSINE-5'-DIPHOSPHATE, IRON/SULFUR CLUSTER, ... (5 entities in total) |
| Functional Keywords | nitrogenase, metalloprotein, iron sulfur cluster, oxidoreductase |
| Biological source | Azotobacter vinelandii |
| Total number of polymer chains | 1 |
| Total formula weight | 32351.39 |
| 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 citation | Buscagan, 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: 35904245DOI: 10.7554/eLife.79311 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.49 Å) |
Structure validation
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