|
|
| Line 3: |
Line 3: |
| | <StructureSection load='2zon' size='340' side='right'caption='[[2zon]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='2zon' size='340' side='right'caption='[[2zon]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2zon]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Achromobacter_xylosoxidans Achromobacter xylosoxidans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZON OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2ZON FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2zon]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Achromobacter_xylosoxidans Achromobacter xylosoxidans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZON 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=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]] 1.7Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitrite_reductase_(NO-forming) Nitrite reductase (NO-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.1 1.7.2.1] </span></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=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://proteopedia.org/fgij/fg.htm?mol=2zon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zon OCA], [http://pdbe.org/2zon PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zon RCSB], [http://www.ebi.ac.uk/pdbsum/2zon PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zon 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=2zon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zon OCA], [https://pdbe.org/2zon PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zon RCSB], [https://www.ebi.ac.uk/pdbsum/2zon PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zon ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O68601_ALCXX O68601_ALCXX] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 37: |
Line 39: |
| | [[Category: Achromobacter xylosoxidans]] | | [[Category: Achromobacter xylosoxidans]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Koteishi, H]] | + | [[Category: Koteishi H]] |
| - | [[Category: Nojiri, M]] | + | [[Category: Nojiri M]] |
| - | [[Category: Suzuki, S]] | + | [[Category: Suzuki S]] |
| - | [[Category: Yamaguchi, K]] | + | [[Category: Yamaguchi K]] |
| - | [[Category: Denitrification]]
| + | |
| - | [[Category: Electron transfer]]
| + | |
| - | [[Category: Nitrite]]
| + | |
| - | [[Category: Oxidoreductase-electron transport complex]]
| + | |
| Structural highlights
Function
O68601_ALCXX
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
Recent earth science studies have pointed out that massive acceleration of the global nitrogen cycle by anthropogenic addition of bio-available nitrogen has led to a host of environmental problems. Nitrous oxide (N(2)O) is a greenhouse gas that is an intermediate during the biological process known as denitrification. Copper-containing nitrite reductase (CuNIR) is a key enzyme in the process; it produces a precursor for N(2)O by catalysing the one-electron reduction of nitrite (NO2-) to nitric oxide (NO). The reduction step is performed by an efficient electron-transfer reaction with a redox-partner protein. However, details of the mechanism during the electron-transfer reaction are still unknown. Here we show the high-resolution crystal structure of the electron-transfer complex for CuNIR with its cognate cytochrome c as the electron donor. The hydrophobic electron-transfer path is formed at the docking interface by desolvation owing to close contact between the two proteins. Structural analysis of the interface highlights an essential role for the loop region with a hydrophobic patch for protein-protein recognition; it also shows how interface construction allows the variation in atomic components to achieve diverse biological electron transfers.
Structural basis of inter-protein electron transfer for nitrite reduction in denitrification.,Nojiri M, Koteishi H, Nakagami T, Kobayashi K, Inoue T, Yamaguchi K, Suzuki S Nature. 2009 Nov 5;462(7269):117-20. PMID:19890332[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nojiri M, Koteishi H, Nakagami T, Kobayashi K, Inoue T, Yamaguchi K, Suzuki S. Structural basis of inter-protein electron transfer for nitrite reduction in denitrification. Nature. 2009 Nov 5;462(7269):117-20. PMID:19890332 doi:10.1038/nature08507
|
