Structural highlights
Function
FER_THEVB Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of Synechococcus elongatus [Fe2S2] ferredoxin in solution.,Baumann B, Sticht H, Scharpf M, Sutter M, Haehnel W, Rosch P Biochemistry. 1996 Oct 1;35(39):12831-41. PMID:8841126[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Baumann B, Sticht H, Scharpf M, Sutter M, Haehnel W, Rosch P. Structure of Synechococcus elongatus [Fe2S2] ferredoxin in solution. Biochemistry. 1996 Oct 1;35(39):12831-41. PMID:8841126 doi:10.1021/bi961144m
