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pubmed-article:8841126pubmed:abstractTextFerredoxins 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.lld:pubmed
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pubmed-article:8841126pubmed:articleTitleStructure of Synechococcus elongatus [Fe2S2] ferredoxin in solution.lld:pubmed
pubmed-article:8841126pubmed:affiliationLehrstuhl für Biopolymere, Universität Bayreuth, Germany.lld:pubmed
pubmed-article:8841126pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:8841126pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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