1ulw: Difference between revisions

Revision as of 09:49, 29 July 2008

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File:1ulw.png

Template:STRUCTURE 1ulw

Crystal structure of P450nor Ser73Gly/Ser75Gly mutantCrystal structure of P450nor Ser73Gly/Ser75Gly mutant

Template:ABSTRACT PUBMED 15313618

About this StructureAbout this Structure

1ULW is a Single protein structure of sequence from Fusarium oxysporum. Full crystallographic information is available from OCA.

ReferenceReference

Structural evidence for direct hydride transfer from NADH to cytochrome P450nor., Oshima R, Fushinobu S, Su F, Zhang L, Takaya N, Shoun H, J Mol Biol. 2004 Sep 3;342(1):207-17. PMID:15313618

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OCA

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-'''Crystal structure of P450nor Ser73Gly/Ser75Gly mutant'''
+===Crystal structure of P450nor Ser73Gly/Ser75Gly mutant===
-==Overview==
+<!--
-Nitric oxide reductase cytochrome P450nor catalyzes an unusual reaction, direct electron transfer from NAD(P)H to bound heme. Here, we succeeded in determining the crystal structure of P450nor in a complex with an NADH analogue, nicotinic acid adenine dinucleotide, which provides conclusive evidence for the mechanism of the unprecedented electron transfer. Comparison of the structure with those of dinucleotide-free forms revealed a global conformational change accompanied by intriguing local movements caused by the binding of the pyridine nucleotide. Arg64 and Arg174 fix the pyrophosphate moiety upon the dinucleotide binding. Stereo-selective hydride transfer from NADH to NO-bound heme was suggested from the structure, the nicotinic acid ring being fixed near the heme by the conserved Thr residue in the I-helix and the upward-shifted propionate side-chain of the heme. A proton channel near the NADH channel is formed upon the dinucleotide binding, which should direct continuous transfer of the hydride and proton. A salt-bridge network (Glu71-Arg64-Asp88) was shown to be crucial for a high catalytic turnover.
+The line below this paragraph, {{ABSTRACT_PUBMED_15313618}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15313618 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15313618}}
 ==About this Structure==
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 [[Category: Cytochrome p450nor]]
 [[Category: Nitric oxide reductase]]
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