1rom
From Proteopedia
(New page: 200px<br /><applet load="1rom" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rom, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF ...) |
|||
Line 1: | Line 1: | ||
- | [[Image:1rom.gif|left|200px]]<br /><applet load="1rom" size=" | + | [[Image:1rom.gif|left|200px]]<br /><applet load="1rom" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rom, resolution 2.0Å" /> | caption="1rom, resolution 2.0Å" /> | ||
'''CRYSTAL STRUCTURE OF NITRIC REDUCTASE FROM DENITRIFYING FUNGUS FUSARIUM OXYSPORUM'''<br /> | '''CRYSTAL STRUCTURE OF NITRIC REDUCTASE FROM DENITRIFYING FUNGUS FUSARIUM OXYSPORUM'''<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== | ||
- | 1ROM 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 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1ROM 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> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ROM OCA]. |
==Reference== | ==Reference== | ||
Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Nakagawa, A.]] | [[Category: Nakagawa, A.]] | ||
- | [[Category: Park, S | + | [[Category: Park, S Y.]] |
[[Category: HEM]] | [[Category: HEM]] | ||
[[Category: cytochrome p450nor]] | [[Category: cytochrome p450nor]] | ||
Line 20: | Line 20: | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:52:59 2008'' |
Revision as of 12:53, 21 February 2008
|
CRYSTAL STRUCTURE OF NITRIC REDUCTASE FROM DENITRIFYING FUNGUS FUSARIUM OXYSPORUM
Overview
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
1ROM is a Single protein structure of sequence from Fusarium oxysporum with as ligand. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 14:52:59 2008