6rxn
From Proteopedia
THE STRUCTURE OF RUBREDOXIN FROM DESULFOVIBRIO DESULFURICANS
Structural highlights
Function[RUBR1_DESDA] 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 PubMedThe structure of a small rubredoxin from the bacterium Desulfovibrio desulfuricans has been determined and refined at 1.5 A resolution. The hairpin loop containing seven residues in other rubredoxins is missing in this 45 residue molecule, and once that fact was determined by amino acid sequencing studies, refinement progressed smoothly to an R value of 0.093 for all reflections from 5 to 1.5 A resolution. Nearly all of the water molecules in the well-ordered triclinic unit cell have been added to the crystallographic model. As in the other refined rubredoxin models, the Fe-S4 complex is slightly distorted from ideal tetrahedral coordination. The structure of rubredoxin from Desulfovibrio desulfuricans strain 27774 at 1.5 A resolution.,Stenkamp RE, Sieker LC, Jensen LH Proteins. 1990;8(4):352-64. PMID:2091025[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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