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Search query: Azotobacter vinelandii
29 articles match your search "Azotobacter vinelandii"Results 1 to 10, sorted by relevance:
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Several Azotobacter iron–sulfur proteins probably play roles in the complex redox chemistry that Azotobacter must maintain when fixing nitrogen. The 2.1 Å resolution crystal structure of the [2Fe–2S] protein I (Shethna protein I) from Azotobacter vinelandii reveals a homodimer similar to the structure of the thioredoxin-like [2Fe–2S] protein from Aquifex aeolicus, with the [2Fe–2S] cluster coordinated by the surrounding conserved cysteine residues.
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The Azotobacter vinelandii FeSII protein forms an oxygen-resistant complex with the nitrogenase MoFe and Fe proteins.
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Crystallization of rhodanese from A. vinelandii is presented.
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Determination of the nitrogenase MoFe protein from C. pasteurianum at 1.08 Å resolution and comparison to its distinct ortholog from A. vinelandii at atomic resolution reveals conserved structural arrangements that are significant to the function of nitrogenase.
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Apo and ligand-bound forms of the cytoplasmic molybdate-binding protein ModG from A. vinelandii have been crystallized in space groups P6322 and P321, respectively. X-ray data were collected on both forms to a maximum resolution of 2.0 Å.
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The PAS domain of the NifL protein from A. vinelandii has been crystallized and X-ray diffraction data have been collected to 3.0 Å using synchrotron radiation. The native crystals belong to space group R32, with unit-cell parameters a = 65.0, c = 157.3 Å.
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The crystal structure of the cytoplasmic cyclophilin A (CyPA) from the bacterium Azotobacter vinelandii complexed with a synthetic tetrapeptide has been determined by molecular replacement at 2 Å resolution.
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Ferredoxin I from Azotobacter vinelandii (AvFdI) is an iron-sulfur protein composed of 106 amino acids, seven Fe atoms and eight inorganic S* atoms. A crystallographic redetermination of its structure showed the originally reported structure to be incorrect. We report here the crystal structure of AvFdI at pH 6.5. Extensive refinement has led to a final R value of 0.170 for all 6986 non-extinct reflections in the range 10-2.3 Å using a solvent model which includes 98 discrete solvent atoms with occupancies between 0.3 and 1.0 and an average B value of 22.5 Å2. The first half of the peptide chain closely resembles that of the 55-residue ferredoxin from Peptococcus aerogenes (PaFd), while the remainder consists of three turns of helix and a series of loops which form a cap over part of the molecular core. Despite the similarities in structure and surroundings, the corresponding 4Fe4S* clusters in PaFd and AvFdI have strikingly different redox potentials; a possible explanation has been sought in the differing hydration models for the two molecules.
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The expression, purification and crystallization of the periplasmic protein AlgX from P. aeruginosa is described. The crystals diffracted to 2.1 Å resolution.
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