1rom
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<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> | <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" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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'>[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> | <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> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1rom ConSurf]. | </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=1rom ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == 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. | ||
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| - | 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<ref>PMID:9334748</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1rom" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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[[Category: Fusarium oxysporum]] | [[Category: Fusarium oxysporum]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Nakagawa | + | [[Category: Nakagawa A]] |
| - | [[Category: Park | + | [[Category: Park S-Y]] |
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Current revision
CRYSTAL STRUCTURE OF NITRIC REDUCTASE FROM DENITRIFYING FUNGUS FUSARIUM OXYSPORUM
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