1rom
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(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 ...)
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Revision as of 23:38, 20 November 2007
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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 HEM 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
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