1cqx

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{{STRUCTURE_1cqx| PDB=1cqx | SCENE= }}
{{STRUCTURE_1cqx| PDB=1cqx | SCENE= }}
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'''Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution'''
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===Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_8557026}}
==About this Structure==
==About this Structure==
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[[Category: Lipid binding protein]]
[[Category: Lipid binding protein]]
[[Category: Six-stranded antiparallel beta sheet]]
[[Category: Six-stranded antiparallel beta sheet]]
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Revision as of 18:10, 30 June 2008

Image:1cqx.png

Template:STRUCTURE 1cqx

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

Template:ABSTRACT PUBMED 8557026

About this Structure

1CQX is a Single protein structure of sequence from Cupriavidus necator. Full crystallographic information is available from OCA.

Reference

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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