2rom: Difference between revisions

Line 1:

[[Image:2rom.gif|left|200px]]<br /><applet load="2rom" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2rom.gif|left|200px]]<br /><applet load="2rom" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2rom, resolution 2.0Å" />

'''CRYSTAL STRUCTURE OF NITRIC REDUCTASE FROM DENITRIFYING FUNGUS FUSARIUM OXYSPORUM COMPLEX WITH CARBON MONOXIDE'''<br />

==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.

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==

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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2ROM OCA].

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==

Line 14:

[[Category: Single protein]]

[[Category: Nakagawa, A.]]

[[Category: Park, S.Y.]]

[[Category: Park, S Y.]]

[[Category: CMO]]

[[Category: HEM]]

Line 21:

[[Category: oxidoreductase]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 13:58:~~28 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:48:48 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2rom.gif|left|200px]]<br /><applet load="2rom" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2rom.gif|left|200px]]<br /><applet load="2rom" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2rom, resolution 2.0&Aring;" />
 '''CRYSTAL STRUCTURE OF NITRIC REDUCTASE FROM DENITRIFYING FUNGUS FUSARIUM OXYSPORUM COMPLEX WITH CARBON MONOXIDE'''<br />
 ==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.
+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==
-ROM 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ROM OCA].
+ROM 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==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Nakagawa, A.]]
-[[Category: Park, S.Y.]]
+[[Category: Park, S Y.]]
 [[Category: CMO]]
 [[Category: HEM]]
@@ Line 21: / Line 21: @@
 [[Category: oxidoreductase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:58:28 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:48:48 2008''