Structural highlights
Function
FER_PYRFU 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
The structure of [Fe(3)S(4)]-ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus has been determined to 1.5 A resolution from a crystal belonging to space group P2(1) with two molecules in the asymmetric unit. The structure has been solved with molecular replacement by use of the ferredoxin from Thermotoga maritima. The fold is similar to that of related monocluster ferredoxins and contains two double-stranded antiparallel beta-sheets and two alpha-helices. The hydrophobic interaction between Trp2 and Tyr46 is confirmed, linking the C-terminus to the longer alpha-helix. The structure contains a double-conformation disulfide bond existing in a left-handed and a right-handed spiral conformation. The crystal packing reveals a beta-sheet interaction, which supports the suggestion that P. furiosus ferredoxin is a functional dimer. The extraordinary thermostability of P. furiosus ferredoxin is further discussed.
The 1.5 A resolution crystal structure of [Fe3S4]-ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus.,Nielsen MS, Harris P, Ooi BL, Christensen HE Biochemistry. 2004 May 11;43(18):5188-94. PMID:15122884[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nielsen MS, Harris P, Ooi BL, Christensen HE. The 1.5 A resolution crystal structure of [Fe3S4]-ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus. Biochemistry. 2004 May 11;43(18):5188-94. PMID:15122884 doi:10.1021/bi049942x
