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Three-dimensional Structure of the Nitrogen Fixation Flavodoxin (NifF) from Rhodobacter capsulatus at 2.2 AThree-dimensional Structure of the Nitrogen Fixation Flavodoxin (NifF) from Rhodobacter capsulatus at 2.2 A
Structural highlights
FunctionFLAV_RHOCB Low-potential electron donor to a number of redox enzymes. NifF is the electron donor to nitrogenase. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAnalysis of the crystal structure of NifF from Rhodobacter capsulatus and its homologues reported so far reflects the existence of unique structural features in nif flavodoxins: a leucine at the re face of the isoalloxazine, an eight-residue insertion at the C-terminus of the 50's loop and a remarkable difference in the electrostatic potential surface with respect to non-nif flavodoxins. A phylogenetic study on 64 sequences from 52 bacterial species revealed four clusters, including different functional prototypes, correlating the previously defined as "short-chain" with the firmicutes flavodoxins and the "long-chain" with gram-negative species. The comparison of Rhodobacter NifF structure with other bacterial flavodoxin prototypes discloses the concurrence of specific features of these functional electron donors to nitrogenase. Structural and Phylogenetic Analysis of Rhodobacter capsulatus NifF: Uncovering General Features of Nitrogen-fixation (nif)-Flavodoxins.,Perez-Dorado I, Bortolotti A, Cortez N, Hermoso JA Int J Mol Sci. 2013 Jan 9;14(1):1152-63. doi: 10.3390/ijms14011152. PMID:23303276[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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