4knt
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4knt]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Nitrosomonas_europaea_ATCC_19718 Nitrosomonas europaea ATCC 19718]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KNT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KNT FirstGlance]. <br> | <table><tr><td colspan='2'>[[4knt]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Nitrosomonas_europaea_ATCC_19718 Nitrosomonas europaea ATCC 19718]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KNT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KNT FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.9Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4knt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4knt OCA], [https://pdbe.org/4knt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4knt RCSB], [https://www.ebi.ac.uk/pdbsum/4knt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4knt 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=4knt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4knt OCA], [https://pdbe.org/4knt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4knt RCSB], [https://www.ebi.ac.uk/pdbsum/4knt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4knt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q82VX5_NITEU Q82VX5_NITEU] | [https://www.uniprot.org/uniprot/Q82VX5_NITEU Q82VX5_NITEU] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Nitrifier denitrification is the conversion of nitrite to nitrous oxide by ammonia oxidizing organisms. This process, which is distinct from denitrification, is active under aerobic conditions in the model nitrifier Nitrosomonas europaea. The central enzyme of the nitrifier dentrification pathway is a copper nitrite reductase (CuNIR). To understand how a CuNIR, typically inactivated by oxygen, functions in this pathway, the enzyme isolated directly from N. europaea (NeNIR) was biochemically and structurally characterized. NeNIR reduces nitrite at a similar rate to other CuNIRs, but appears to be oxygen tolerant. Crystal structures of oxidized and reduced NeNIR reveal a substrate channel to the active site that is much more restricted than channels in typical CuNIRs. In addition, there is a second fully hydrated channel leading to the active site that likely acts a water exit pathway. The structure is minimally affected by changes in pH. Taken together, these findings provide insight into the molecular basis for NeNIR oxygen tolerance. | ||
| - | + | ==See Also== | |
| - | + | *[[Nitrite reductase 3D structures|Nitrite reductase 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Copper nitrite reductase from Nitrosomonas europaea pH 8.5
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