Biomaterial Database

Structure of Azotobacter vinelandii 7Fe ferredoxin. Amino acid sequence and electron density maps of residues. 1983

J B Howard, and T W Lorsbach, and D Ghosh, and K Melis, and C D Stout

The complete amino acid sequence of the 7Fe ferredoxin from Azotobacter vinelandii (Av Fd) was determined by repetitive Edman degradation of the whole protein and of peptides derived from CNBr cleavage or chymotrypsin digestion. The sequence was confirmed by the 2A electron density maps for the residues calculated with difference Fourier coefficients. The density maps for all residues are included in the paper. Av Fd has several important differences with the clostridial-type ferredoxins: (i) Av Fd is 106 residues (versus 55-60 for other bacterial ferredoxins); (ii) Av Fd has 9 cysteines, one of which (residue 24) is not homologous with the bacterial ferredoxins; (iii) Av Fd has 2 extra residues between 2 cysteines (residues 11 and 16) homologous to cysteines in the bacterial ferredoxins; and (iv) Av Fd has the unique sequence -Cys-Val-Glu-Val-Cys- (residues 16-20) which are two of the ligands of the 3Fe:3S center. These sequence features are compared to the sequences of various ferredoxin groups. Structure predictions for other suspected 7Fe ferredoxins are discussed.

UI	MeSH Term	Description	Entries
D008958	Models, Molecular	Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.	Molecular Models,Model, Molecular,Molecular Model
D010446	Peptide Fragments	Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.	Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D011487	Protein Conformation	The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).	Conformation, Protein,Conformations, Protein,Protein Conformations
D005288	Ferredoxins	Iron-containing proteins that transfer electrons, usually at a low potential, to flavoproteins; the iron is not present as in heme. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)	Ferredoxin,Ferredoxin I,Ferredoxin II,Ferredoxin III
D005583	Fourier Analysis	Analysis based on the mathematical function first formulated by Jean-Baptiste-Joseph Fourier in 1807. The function, known as the Fourier transform, describes the sinusoidal pattern of any fluctuating pattern in the physical world in terms of its amplitude and its phase. It has broad applications in biomedicine, e.g., analysis of the x-ray crystallography data pivotal in identifying the double helical nature of DNA and in analysis of other molecules, including viruses, and the modified back-projection algorithm universally used in computerized tomography imaging, etc. (From Segen, The Dictionary of Modern Medicine, 1992)	Fourier Series,Fourier Transform,Analysis, Cyclic,Analysis, Fourier,Cyclic Analysis,Analyses, Cyclic,Cyclic Analyses,Series, Fourier,Transform, Fourier
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001395	Azotobacter	A genus of gram-negative, aerobic bacteria found in soil and water. Its organisms occur singly, in pairs or irregular clumps, and sometimes in chains of varying lengths.