1cqx
Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution
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OverviewOverview
The molecular structure of the flavohemoglobin from Alcaligenes eutrophus, has been determined to a resolution of 1.75 A and refined to an R-factor, of 19.6%. The protein comprises two fused modules: a heme binding module, which belongs to the globin family, and an FAD binding oxidoreductase, module, which adopts a fold like ferredoxin reductase. The most striking, deviation of the bacterial globin structure from those of other species is, the movement of helix E in a way to provide more space in the vicinity of, the distal heme binding site. A comparison with other members of the, ferredoxin reductase family shows similar tertiary structures for the, individual FAD and NAD binding domains but largely different interdomain, orientations. The heme and FAD molecules approach each other to a minimal, distance of 6.3 A and adopt an interplanar angle of 80 degrees. The, electron transfer from FAD to heme occurs in a predominantly polar, environment and may occur directly or be mediated by a water molecule.
About this StructureAbout this Structure
1CQX is a Single protein structure of sequence from Cupriavidus necator with NA, HEM, FAD and DGG as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution., Ermler U, Siddiqui RA, Cramm R, Friedrich B, EMBO J. 1995 Dec 15;14(24):6067-77. PMID:8557026
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