1snr
From Proteopedia
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==Nitric oxide bound to Cu nitrite reductase== | ==Nitric oxide bound to Cu nitrite reductase== | ||
| - | <StructureSection load='1snr' size='340' side='right' caption='[[1snr]], [[Resolution|resolution]] 1.31Å' scene=''> | + | <StructureSection load='1snr' size='340' side='right'caption='[[1snr]], [[Resolution|resolution]] 1.31Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | [[1snr]] is a 3 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1snr]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SNR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SNR FirstGlance]. <br> |
| - | <b> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.31Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=NO:NITRIC+OXIDE'>NO</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=1snr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1snr OCA], [https://pdbe.org/1snr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1snr RCSB], [https://www.ebi.ac.uk/pdbsum/1snr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1snr ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/NIR_ALCFA NIR_ALCFA] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| - | [[Image:Consurf_key_small.gif|right]] | + | [[Image:Consurf_key_small.gif|200px|right]] |
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sn/1snr_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sn/1snr_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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=1snr ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | == Publication Abstract from PubMed == | ||
| - | A copper-nitrosyl intermediate forms during the catalytic cycle of nitrite reductase, the enzyme that mediates the committed step in bacterial denitrification. The crystal structure of a type 2 copper-nitrosyl complex of nitrite reductase reveals an unprecedented side-on binding mode in which the nitrogen and oxygen atoms are nearly equidistant from the copper cofactor. Comparison of this structure with a refined nitrite-bound crystal structure explains how coordination can change between copper-oxygen and copper-nitrogen during catalysis. The side-on copper-nitrosyl in nitrite reductase expands the possibilities for nitric oxide interactions in copper proteins such as superoxide dismutase and prions. | ||
| - | |||
| - | Side-on copper-nitrosyl coordination by nitrite reductase.,Tocheva EI, Rosell FI, Mauk AG, Murphy ME Science. 2004 May 7;304(5672):867-70. PMID:15131305<ref>PMID:15131305</ref> | ||
| - | + | ==See Also== | |
| - | == | + | *[[Nitrite reductase 3D structures|Nitrite reductase 3D structures]] |
| - | + | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Alcaligenes faecalis]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Mauk AG]] |
| - | [[Category: | + | [[Category: Murphy ME]] |
| - | [[Category: | + | [[Category: Rosell FI]] |
| - | [[Category: | + | [[Category: Tocheva EI]] |
| - | + | ||
| - | + | ||
Current revision
Nitric oxide bound to Cu nitrite reductase
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