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Crystal structure of the [2Fe–2S] protein I (Shethna protein I) from Azotobacter vinelandii

DOI: 10.1107/S2053230X21009936 DOI Help

Authors: Burak V. Kabasakal (Imperial College London; Ankara University) , Charles A. R. Cotton (Imperial College London; Cambrium GmbH) , James W. Murray (Imperial College London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 77 , PAGES 407 - 411

State: Published (Approved)
Published: November 2021
Diamond Proposal Number(s): 9424

Open Access Open Access

Abstract: Azotobacter vinelandii is a model diazotroph and is the source of most nitrogenase material for structural and biochemical work. Azotobacter can grow in above-atmospheric levels of oxygen, despite the sensitivity of nitrogenase activity to oxygen. Azotobacter has many iron–sulfur proteins in its genome, which were identified as far back as the 1960s and probably play roles in the complex redox chemistry that Azotobacter must maintain when fixing nitrogen. Here, the 2.1 Å resolution crystal structure of the [2Fe–2S] protein I (Shethna protein I) from A. vinelandii is presented, revealing a homodimer with the [2Fe–2S] cluster coordinated by the surrounding conserved cysteine residues. It is similar to the structure of the thioredoxin-like [2Fe–2S] protein from Aquifex aeolicus, including the positions of the [2Fe–2S] clusters and conserved cysteine residues. The structure of Shethna protein I will provide information for understanding its function in relation to nitrogen fixation and its evolutionary relationships to other ferredoxins.

Journal Keywords: iron–sulfur proteins; Shethna protein I; Azotobacter vinelandii

Diamond Keywords: Bacteria

Subject Areas: Biology and Bio-materials

Instruments: I03-Macromolecular Crystallography , I04-Macromolecular Crystallography

Added On: 03/11/2021 09:17


Discipline Tags:

Life Sciences & Biotech Structural biology

Technical Tags:

Diffraction Macromolecular Crystallography (MX)