title: Solution structure of ferredoxin from the thermophilic cyanobacterium Synechococcus elongatus and its thermostability.
abstract: The three-dimensional structure of ferredoxin, purified from the thermophilic cyanobacterium Synechococcus elongatus, was determined in aqueous solution by two-dimensional proton nuclear magnetic resonance. In addition to the 946 distance constraints from nuclear Overhauser effect connectivities, we added 241 distance constraints derived from the crystal structure of Spirulina platensis ferredoxin to the 19 residues close to the [2Fe-2S] iron-sulfur center, where crosspeaks disappeared due to paramagnetic effects. The atomic root-mean-square difference of the ten converged structures from the mean structure was 0.61(+/-0.12) A for backbone atoms (N, C(alpha), C'). The main-chain structure was almost the same as the crystal structures of other mesophile ferredoxins, but comparison of the side-chain structures revealed an extension of the hydrophobic core, a unique hydrophobic patch on the surface of the large beta-sheet, and two unique charge networks in this thermostable ferredoxin structure, some of which might contribute to thermostability.
authors.affiliation: Department of Molecular Physiology, The Tokyo Metropolitan Institute of Medical Science, Bunkyo-ku, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Hatanaka
authors.forename: R
authors.initials: R
authors.lastname: Tanimura
authors.forename: S
authors.initials: S
authors.lastname: Katoh
authors.forename: F
authors.initials: F
authors.lastname: Inagaki
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D000458:Cyanobacteria / Q000737:chemistry*; D005288:Ferredoxins / Q000737:chemistry* / Q000378:metabolism; D006358:Hot Temperature; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D012996:Solutions; D055672:Static Electricity
chemical_list: D005288:Ferredoxins; D012996:Solutions