2rom: Difference between revisions
New page: left|200px<br /><applet load="2rom" size="450" color="white" frame="true" align="right" spinBox="true" caption="2rom, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF ... |
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[[Image:2rom.gif|left|200px]]<br /><applet load="2rom" size=" | [[Image:2rom.gif|left|200px]]<br /><applet load="2rom" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2rom, resolution 2.0Å" /> | caption="2rom, resolution 2.0Å" /> | ||
'''CRYSTAL STRUCTURE OF NITRIC REDUCTASE FROM DENITRIFYING FUNGUS FUSARIUM OXYSPORUM COMPLEX WITH CARBON MONOXIDE'''<br /> | '''CRYSTAL STRUCTURE OF NITRIC REDUCTASE FROM DENITRIFYING FUNGUS FUSARIUM OXYSPORUM COMPLEX WITH CARBON MONOXIDE'''<br /> | ||
==Overview== | ==Overview== | ||
Structures of nitric oxide reductase (NOR) in the ferric resting and the | Structures of nitric oxide reductase (NOR) in the ferric resting and the ferrous CO states have been solved at 2.0 A resolution. These structures provide significant new insights into how NO is reduced in biological systems. The haem distal pocket is open to solvent, implicating this region as a possible NADH binding site. In combination with mutagenesis results, a hydrogen-bonding network from the water molecule adjacent to the iron ligand to the protein surface of the distal pocket through the hydroxyl group of Ser 286 and the carboxyl group of Asp 393 can be assigned to a pathway for proton delivery during the NO reduction reaction. | ||
==About this Structure== | ==About this Structure== | ||
2ROM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum] with HEM and CMO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 2ROM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=CMO:'>CMO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ROM OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Nakagawa, A.]] | [[Category: Nakagawa, A.]] | ||
[[Category: Park, S | [[Category: Park, S Y.]] | ||
[[Category: CMO]] | [[Category: CMO]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:48:48 2008'' | ||
Revision as of 19:48, 21 February 2008
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CRYSTAL STRUCTURE OF NITRIC REDUCTASE FROM DENITRIFYING FUNGUS FUSARIUM OXYSPORUM COMPLEX WITH CARBON MONOXIDE
OverviewOverview
Structures of nitric oxide reductase (NOR) in the ferric resting and the ferrous CO states have been solved at 2.0 A resolution. These structures provide significant new insights into how NO is reduced in biological systems. The haem distal pocket is open to solvent, implicating this region as a possible NADH binding site. In combination with mutagenesis results, a hydrogen-bonding network from the water molecule adjacent to the iron ligand to the protein surface of the distal pocket through the hydroxyl group of Ser 286 and the carboxyl group of Asp 393 can be assigned to a pathway for proton delivery during the NO reduction reaction.
About this StructureAbout this Structure
2ROM is a Single protein structure of sequence from Fusarium oxysporum with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of nitric oxide reductase from denitrifying fungus Fusarium oxysporum., Park SY, Shimizu H, Adachi S, Nakagawa A, Tanaka I, Nakahara K, Shoun H, Obayashi E, Nakamura H, Iizuka T, Shiro Y, Nat Struct Biol. 1997 Oct;4(10):827-32. PMID:9334748
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