ArticleActa crystallographica. Section D, Biological crystallography2015
Nitrogenase MoFe protein from Clostridium pasteurianum at 1.08 Å resolution: comparison with the Azotobacter vinelandii MoFe protein.
Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Article
- Molecular basis of NNature communications · 2026Article
- Function, Structure, and Regulation of Nitrogen Fixation-like Metalloproteins for Nitrogen, Energy, Carbon, and Sulfur Metabolism.Chemical reviews · 2026Review
- Deserts, Rivers, Pools, and Billabongs: Water Features of the Nitrogenase Proteins, and their Functions.Chembiochem : a European journal of chemical biology · 2025Review
- Single-Step Insertion of Organic Sulfur Into a FeAngewandte Chemie (International ed. in English) · 2025Article
- Structures of the nitrogenase complex prepared under catalytic turnover conditions.Science (New York, N.Y.) · 2022Article
- Phylogenetically and catabolically diverse diazotrophs reside in deep-sea cold seep sediments.Nature communications · 2022Article
- Statistical analysis of PRSC advances · 2022Article
- Conformationally Gated Electron Transfer in Nitrogenase. Isolation, Purification, and Characterization of Nitrogenase From Gluconacetobacter diazotrophicus.Methods in enzymology · 2018Article
- Reversible Protonated Resting State of the Nitrogenase Active Site.Journal of the American Chemical Society · 2017Article
- Elucidating reaction mechanisms on quantum computers.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Systematic analysis of residual density suggests that a major limitation in well-refined X-ray structures of proteins is the omission of ordered solvent.Protein science : a publication of the Protein Society · 2017Article
- Production and isolation of vanadium nitrogenase from Azotobacter vinelandii by molybdenum depletion.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Article
- Tyrosine-Coordinated P-Cluster in G. diazotrophicus Nitrogenase: Evidence for the Importance of O-Based Ligands in Conformationally Gated Electron Transfer.Journal of the American Chemical Society · 2016Article
- Insight into the Iron-Molybdenum Cofactor of Nitrogenase from Synthetic Iron Complexes with Sulfur, Carbon, and Hydride Ligands.Journal of the American Chemical Society · 2016Review
- Two distinct modes of metal ion binding in the nuclease active site of a viral DNA-packaging terminase: insight into the two-metal-ion catalytic mechanism.Nucleic acids research · 2015Article
- Substrate pathways in the nitrogenase MoFe protein by experimental identification of small molecule binding sites.Biochemistry · 2015Article
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4 authors.
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Abstract
The X-ray crystal structure of the nitrogenase MoFe protein from Clostridium pasteurianum (Cp1) has been determined at 1.08 Å resolution by multiwavelength anomalous diffraction phasing. Cp1 and the ortholog from Azotobacter vinelandii (Av1) represent two distinct families of nitrogenases, differing primarily by a long insertion in the α-subunit and a deletion in the β-subunit of Cp1 relative to Av1. Comparison of these two MoFe protein structures at atomic resolution reveals conserved structural arrangements that are significant to the function of nitrogenase. The FeMo cofactors defining the active sites of the MoFe protein are essentially identical between the two proteins. The surrounding environment is also highly conserved, suggesting that this structural arrangement is crucial for nitrogen reduction. The P clusters are likewise similar, although the surrounding protein and solvent environment is less conserved relative to that of the FeMo cofactor. The P cluster and FeMo cofactor in Av1 and Cp1 are connected through a conserved water tunnel surrounded by similar secondary-structure elements. The long α-subunit insertion loop occludes the presumed Fe protein docking surface on Cp1 with few contacts to the remainder of the protein. This makes it plausible that this loop is repositioned to open up the Fe protein docking surface for complex formation.
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