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1xqd

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[[Image:1xqd.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of P450NOR complexed with 3-pyridinealdehyde adenine dinucleotide==
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|PDB= 1xqd |SIZE=350|CAPTION= <scene name='initialview01'>1xqd</scene>, resolution 1.80&Aring;
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<StructureSection load='1xqd' size='340' side='right'caption='[[1xqd]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=DND:NICOTINIC ACID ADENINE DINUCLEOTIDE'>DND</scene>
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<table><tr><td colspan='2'>[[1xqd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XQD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XQD FirstGlance]. <br>
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|ACTIVITY= [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]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DND:NICOTINIC+ACID+ADENINE+DINUCLEOTIDE'>DND</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xqd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xqd OCA], [https://pdbe.org/1xqd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xqd RCSB], [https://www.ebi.ac.uk/pdbsum/1xqd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xqd ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NOR_FUSOX NOR_FUSOX] Nitric oxide reductase which is involved in a dissimilatory reduction of nitrite. Acts as a nitric oxide reductase. Is able to reduce nitrate and nitrite to a gaseous form of N(2)O when oxygen supply is limited or discontinued. May function as a detoxification mechanism.<ref>PMID:2040619</ref> <ref>PMID:12105197</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xq/1xqd_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xqd ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Crystal structure of P450NOR complexed with 3-pyridinealdehyde adenine dinucleotide'''
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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<ref>PMID:15313618</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1xqd" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1XQD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XQD OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15313618 15313618]
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[[Category: Fusarium oxysporum]]
[[Category: Fusarium oxysporum]]
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[[Category: Nitric-oxide reductase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Fushinobu S]]
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[[Category: Fushinobu, S.]]
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[[Category: Oshima R]]
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[[Category: Oshima, R.]]
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[[Category: Shoun H]]
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[[Category: Shoun, H.]]
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[[Category: Su F]]
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[[Category: Su, F.]]
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[[Category: Takaya N]]
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[[Category: Takaya, N.]]
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[[Category: Wakagi T]]
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[[Category: Wakagi, T.]]
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[[Category: DND]]
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[[Category: HEM]]
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[[Category: cytochrome p450nor]]
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[[Category: nadh complex]]
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[[Category: nitric oxide reductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:13:12 2008''
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Current revision

Crystal structure of P450NOR complexed with 3-pyridinealdehyde adenine dinucleotide

PDB ID 1xqd

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