1CQX

Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution

Summary for 1CQX

• Entry DOI: 10.2210/pdb1cqx/pdb
• Descriptor: FLAVOHEMOPROTEIN, SODIUM ION, PROTOPORPHYRIN IX CONTAINING FE, ... (6 entities in total)
• Functional Keywords: globin fold, six-stranded antiparallel beta sheet, helix-flanked five-stranded parallel beta sheet, lipid binding protein
• Biological source: Cupriavidus necator
• Cellular location: Cytoplasm: P39662
• Total number of polymer chains: 2
• Total formula weight: 93988.82

Authors

Ermler, U.,Siddiqui, R.A.,Cramm, R.,Friedrich, B. (deposition date: 1999-08-12, release date: 1999-08-31, Last modification date: 2024-02-07)

Primary citation

Ermler, U.,Siddiqui, R.A.,Cramm, R.,Friedrich, B.
Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution.
EMBO J., 14:6067-6077, 1995

PubMed Abstract: 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.

PubMed: 8557026

Experimental method

X-RAY DIFFRACTION (1.75 Å)