1xqd: Difference between revisions

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[[Image:1xqd.jpg|left|200px]]
{{Seed}}
[[Image:1xqd.png|left|200px]]


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{{STRUCTURE_1xqd|  PDB=1xqd  |  SCENE=  }}  
{{STRUCTURE_1xqd|  PDB=1xqd  |  SCENE=  }}  


'''Crystal structure of P450NOR complexed with 3-pyridinealdehyde adenine dinucleotide'''
===Crystal structure of P450NOR complexed with 3-pyridinealdehyde adenine dinucleotide===




==Overview==
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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
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{{ABSTRACT_PUBMED_15313618}}


==About this Structure==
==About this Structure==
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[[Category: Nadh complex]]
[[Category: Nadh complex]]
[[Category: Nitric oxide reductase]]
[[Category: Nitric oxide reductase]]
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