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| {{STRUCTURE_1ulw| PDB=1ulw | SCENE= }} | | {{STRUCTURE_1ulw| PDB=1ulw | SCENE= }} |
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| '''Crystal structure of P450nor Ser73Gly/Ser75Gly mutant'''
| | ===Crystal structure of P450nor Ser73Gly/Ser75Gly mutant=== |
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| ==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 |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15313618 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15313618}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Cytochrome p450nor]] | | [[Category: Cytochrome p450nor]] |
| [[Category: Nitric oxide reductase]] | | [[Category: Nitric oxide reductase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:24:25 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:49:45 2008'' |
