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[[Image:1xqd.jpg|left|200px]]
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{{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==
<StructureSection load='1xqd' size='340' side='right'caption='[[1xqd]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Function ==
[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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xq/1xqd_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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].
</div>
<div class="pdbe-citations 1xqd" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Fusarium oxysporum]]
[[Category: Fusarium oxysporum]]
[[Category: Nitric-oxide reductase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Fushinobu S]]
[[Category: Fushinobu, S.]]
[[Category: Oshima R]]
[[Category: Oshima, R.]]
[[Category: Shoun H]]
[[Category: Shoun, H.]]
[[Category: Su F]]
[[Category: Su, F.]]
[[Category: Takaya N]]
[[Category: Takaya, N.]]
[[Category: Wakagi T]]
[[Category: Wakagi, T.]]
[[Category: Cytochrome p450nor]]
[[Category: Nadh complex]]
[[Category: Nitric oxide reductase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 15:22:06 2008''
Retrieved from "https://proteopedia.org/1xqd"