2rom

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Revision as of 14:51, 21 November 2007 by OCA (talk | contribs) (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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File:2rom.gif


2rom, resolution 2.0Å

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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 HEM and CMO 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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