title: Structure of Synechococcus elongatus [Fe2S2] ferredoxin in solution.
abstract: Ferredoxins of the [Fe2S2] type function in photosynthetic electron transport as essential electron acceptors of photosystem I. The solution structure of the 97 amino acid ferredoxin from the thermophilic cyanobacterium Synechococcus elongatus was determined by nuclear magnetic resonance spectroscopy and restrained molecular dynamics calculations. The structure consists of a four-stranded parallel/ antiparallel beta-sheet, a short two-stranded antiparallel beta-sheet, and three short helices. The overall structure is similar to the structure of the ferredoxin from Anabaena. In contrast to related ferredoxins from mesophilic organisms, this thermostable protein contains a salt bridge inside a 17-amino acid hydrophobic core.
authors.affiliation: Lehrstuhl für Biopolymere, Universität Bayreuth, Germany.
authors.forename: B
authors.initials: B
authors.lastname: Baumann
authors.forename: H
authors.initials: H
authors.lastname: Sticht
authors.forename: M
authors.initials: M
authors.lastname: Schärpf
authors.forename: M
authors.initials: M
authors.lastname: Sutter
authors.forename: W
authors.initials: W
authors.lastname: Haehnel
authors.forename: P
authors.initials: P
authors.lastname: Rösch
mesh_terms: D000595:Amino Acid Sequence; D017033:Anabaena / Q000737:chemistry; D003198:Computer Simulation; D000458:Cyanobacteria / Q000737:chemistry*; D004579:Electron Transport; D005288:Ferredoxins / Q000737:chemistry*; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D012997:Solvents; D013056:Spectrophotometry, Ultraviolet
chemical_list: D005288:Ferredoxins; D012997:Solvents