1cqx
From Proteopedia
(New page: 200px<br /><applet load="1cqx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cqx, resolution 1.75Å" /> '''Crystal structure of...) |
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| - | [[Image:1cqx.jpg|left|200px]]<br /><applet load="1cqx" size=" | + | [[Image:1cqx.jpg|left|200px]]<br /><applet load="1cqx" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cqx, resolution 1.75Å" /> | caption="1cqx, resolution 1.75Å" /> | ||
'''Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution'''<br /> | '''Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The molecular structure of the flavohemoglobin from Alcaligenes eutrophus | + | 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 Structure== | ==About this Structure== | ||
| - | 1CQX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cupriavidus_necator Cupriavidus necator] with NA, HEM, FAD and DGG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1CQX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cupriavidus_necator Cupriavidus necator] with <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=DGG:'>DGG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CQX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ermler, U.]] | [[Category: Ermler, U.]] | ||
[[Category: Friedrich, B.]] | [[Category: Friedrich, B.]] | ||
| - | [[Category: Siddiqui, R | + | [[Category: Siddiqui, R A.]] |
[[Category: DGG]] | [[Category: DGG]] | ||
[[Category: FAD]] | [[Category: FAD]] | ||
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[[Category: six-stranded antiparallel beta sheet]] | [[Category: six-stranded antiparallel beta sheet]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:08:51 2008'' |
Revision as of 10:08, 21 February 2008
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Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution
Overview
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 Structure
1CQX is a Single protein structure of sequence from Cupriavidus necator with , , and as ligands. 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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