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1rom

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Revision as of 07:19, 22 September 2021

CRYSTAL STRUCTURE OF NITRIC REDUCTASE FROM DENITRIFYING FUNGUS FUSARIUM OXYSPORUM

Structural highlights

1rom is a 1 chain structure with sequence from Fusarium oxysporum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Structures of nitric oxide reductase (NOR) in the ferric resting and the ferrous CO states have been solved at 2.0 A resolution. These structures provide significant new insights into how NO is reduced in biological systems. The haem distal pocket is open to solvent, implicating this region as a possible NADH binding site. In combination with mutagenesis results, a hydrogen-bonding network from the water molecule adjacent to the iron ligand to the protein surface of the distal pocket through the hydroxyl group of Ser 286 and the carboxyl group of Asp 393 can be assigned to a pathway for proton delivery during the NO reduction reaction.

Crystal structure of nitric oxide reductase from denitrifying fungus Fusarium oxysporum.,Park SY, Shimizu H, Adachi S, Nakagawa A, Tanaka I, Nakahara K, Shoun H, Obayashi E, Nakamura H, Iizuka T, Shiro Y Nat Struct Biol. 1997 Oct;4(10):827-32. PMID:9334748^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Shoun H, Tanimoto T. Denitrification by the fungus Fusarium oxysporum and involvement of cytochrome P-450 in the respiratory nitrite reduction. J Biol Chem. 1991 Jun 15;266(17):11078-82. PMID:2040619
↑ Zhang L, Kudo T, Takaya N, Shoun H. The B' helix determines cytochrome P450nor specificity for the electron donors NADH and NADPH. J Biol Chem. 2002 Sep 13;277(37):33842-7. Epub 2002 Jul 8. PMID:12105197 doi:http://dx.doi.org/10.1074/jbc.M203923200
↑ Park SY, Shimizu H, Adachi S, Nakagawa A, Tanaka I, Nakahara K, Shoun H, Obayashi E, Nakamura H, Iizuka T, Shiro Y. Crystal structure of nitric oxide reductase from denitrifying fungus Fusarium oxysporum. Nat Struct Biol. 1997 Oct;4(10):827-32. PMID:9334748

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1rom"

@@ Line 3: / Line 3: @@
 <StructureSection load='1rom' size='340' side='right'caption='[[1rom]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1rom]] is a 1 chain structure with 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=1ROM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ROM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1rom]] 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=1ROM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ROM FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rom OCA], [http://pdbe.org/1rom PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rom RCSB], [http://www.ebi.ac.uk/pdbsum/1rom PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rom ProSAT]</span></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=1rom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rom OCA], [https://pdbe.org/1rom PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rom RCSB], [https://www.ebi.ac.uk/pdbsum/1rom PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rom ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[[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]]

1rom

From Proteopedia

Revision as of 07:19, 22 September 2021

CRYSTAL STRUCTURE OF NITRIC REDUCTASE FROM DENITRIFYING FUNGUS FUSARIUM OXYSPORUM

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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