1ulw
From Proteopedia
(New page: 200px<br /><applet load="1ulw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ulw, resolution 2.00Å" /> '''Crystal structure of...) |
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| - | [[Image:1ulw.jpg|left|200px]]<br /><applet load="1ulw" size=" | + | [[Image:1ulw.jpg|left|200px]]<br /><applet load="1ulw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ulw, resolution 2.00Å" /> | caption="1ulw, resolution 2.00Å" /> | ||
'''Crystal structure of P450nor Ser73Gly/Ser75Gly mutant'''<br /> | '''Crystal structure of P450nor Ser73Gly/Ser75Gly mutant'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Nitric oxide reductase cytochrome P450nor catalyzes an unusual reaction, direct electron transfer from NAD(P)H to bound heme. Here, we succeeded in | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1ULW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Nitric-oxide_reductase Nitric-oxide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.99.7 1.7.99.7] Full crystallographic information is available from [http:// | + | 1ULW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Nitric-oxide_reductase Nitric-oxide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.99.7 1.7.99.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ULW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: nitric oxide reductase]] | [[Category: nitric oxide reductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:25:56 2008'' |
Revision as of 13:25, 21 February 2008
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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.
About this Structure
1ULW is a Single protein structure of sequence from Fusarium oxysporum with as ligand. Active as Nitric-oxide reductase, with EC number 1.7.99.7 Full crystallographic information is available from OCA.
Reference
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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