Structure of Synechococcus elongatus [Fe2S2] Ferredoxin in Solution
| Autor: | Wolfgang Haehnel, Bettina Baumann, Paul Rösch, Martin Sutter, Manuela Schärpf, Heinrich Sticht |
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| Rok vydání: | 1996 |
| Předmět: |
Models
Molecular inorganic chemicals Magnetic Resonance Spectroscopy Protein Conformation Molecular Sequence Data macromolecular substances Cyanobacteria Antiparallel (biochemistry) Biochemistry Mass Spectrometry Protein Structure Secondary Electron Transport Computer Simulation Amino Acid Sequence Ferredoxin Photosystem chemistry.chemical_classification biology Anabaena Thermophile Hydrogen Bonding Nuclear magnetic resonance spectroscopy Electron acceptor biology.organism_classification Electron transport chain enzymes and coenzymes (carbohydrates) Crystallography chemistry Solvents Ferredoxins bacteria Spectrophotometry Ultraviolet Sequence Alignment |
| Zdroj: | Biochemistry. 35:12831-12841 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi961144m |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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