Structural highlights
Function
[RUBR_DESVM] Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. Electron acceptor for cytoplasmic lactate dehydrogenase.
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 structures of two crystal forms (form I, P3221, a = b = 43.7, c = 50.7 A; form II, P21, a = 27.3, b = 44.9, c = 51.2 A and beta = 90. 6 degrees ) of the rubredoxin from Desulfovibrio vulgaris Miyazaki F have been solved by the molecular-replacement method. Form I has been refined at a resolution of 2.0 A to an R value of 20.8% and includes 32 water molecules. Form II includes 86 water molecules and has been refined at 1.9 A resolution to an R value of 17.5%. In form II, there are three molecules in the asymmetric unit with the molecules related by a non-crystallographic 32 symmetry axis. In both crystal forms, it was found that only a few residues effectively participate in the formation of intermolecular contacts along both the crystallographic (form I) and the non-crystallographic (form II) 32 axes. The crystal structure of the form II crystal is compared with those of other rubredoxin molecules from anaerobic bacteria. From this comparison, a similarity in the core region, which is composed of aromatic residues and includes the active centre, has been revealed.
Structure determination of rubredoxin from Desulfovibrio vulgaris Miyazaki F in two crystal forms.,Misaki S, Morimoto Y, Ogata M, Yagi T, Higuchi Y, Yasuoka N Acta Crystallogr D Biol Crystallogr. 1999 Feb;55(Pt 2):408-13. PMID:10089348[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Misaki S, Morimoto Y, Ogata M, Yagi T, Higuchi Y, Yasuoka N. Structure determination of rubredoxin from Desulfovibrio vulgaris Miyazaki F in two crystal forms. Acta Crystallogr D Biol Crystallogr. 1999 Feb;55(Pt 2):408-13. PMID:10089348
