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| | <StructureSection load='1cno' size='340' side='right'caption='[[1cno]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='1cno' size='340' side='right'caption='[[1cno]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1cno]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Marinobacter_hydrocarbonoclasticus Marinobacter hydrocarbonoclasticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CNO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CNO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1cno]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Marinobacter_nauticus Marinobacter nauticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CNO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CNO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</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]] 2.2Å</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=1cno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cno OCA], [http://pdbe.org/1cno PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cno RCSB], [http://www.ebi.ac.uk/pdbsum/1cno PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cno ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</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=1cno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cno OCA], [https://pdbe.org/1cno PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cno RCSB], [https://www.ebi.ac.uk/pdbsum/1cno PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cno ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CY552_MARHY CY552_MARHY]] Electron donor for periplasmic nitrate reductase. | + | [https://www.uniprot.org/uniprot/CY552_MARNT CY552_MARNT] Electron donor for periplasmic nitrate reductase. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cn/1cno_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cn/1cno_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | ==See Also== | | ==See Also== |
| - | *[[Nitrite reductase|Nitrite reductase]] | + | *[[Cytochrome c nitrite reductase|Cytochrome c nitrite reductase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Marinobacter hydrocarbonoclasticus]] | + | [[Category: Marinobacter nauticus]] |
| - | [[Category: Brown, K]] | + | [[Category: Brown K]] |
| - | [[Category: Cambillau, C]] | + | [[Category: Cambillau C]] |
| - | [[Category: Nurizzo, D]] | + | [[Category: Nurizzo D]] |
| - | [[Category: Cytochrome c]]
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| - | [[Category: Electron transport]]
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| - | [[Category: Heme]]
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| - | [[Category: Multiwavelength anomalous dispersion]]
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| - | [[Category: Pseudomonas nautica]]
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| - | [[Category: X ray structure]]
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| Structural highlights
Function
CY552_MARNT Electron donor for periplasmic nitrate reductase.
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
The monohemic cytochrome c552from Pseudomonas nautica (c552-Pn) is thought to be the electron donor to cytochrome cd1, the so-called nitrite reductase (NiR). It shows as high levels of activity and affinity for the P. nautica NiR (NiR-Pn), as the Pseudomonas aeruginosa enzyme (NiR-Pa). Since cytochrome c552is by far the most abundant electron carrier in the periplasm, it is probably involved in numerous other reactions. Its sequence is related to that of the c type cytochromes, but resembles that of the dihemic c4cytochromes even more closely.The three-dimensional structure of P. nautica cytochrome c552has been solved to 2.2 A resolution using the multiple wavelength anomalous dispersion (MAD) technique, taking advantage of the presence of the eight Fe heme ions in the asymmetric unit. Density modification procedures involving 4-fold non-crystallographic averaging yielded a model with an R -factor value of 17.8 % (Rfree=20.8 %). Cytochrome c552forms a tight dimer in the crystal, and the dimer interface area amounts to 19% of the total cytochrome surface area. Four tighly packed dimers form the eight molecules of the asymmetric unit.The c552dimer is superimposable on each domain of the monomeric cytochrome c4from Pseudomomas stutzeri (c4-Ps), a dihemic cytochrome, and on the dihemic c domain of flavocytochrome c of Chromatium vinosum (Fcd-Cv). The interacting residues which form the dimer are both similar in character and position, which is also true for the propionates. The dimer observed in the crystal also exists in solution. It has been hypothesised that the dihemic c4-Ps may have evolved via monohemic cytochrome c gene duplication followed by evolutionary divergence and the adjunction of a connecting linker. In this process, our dimeric c552structure might be said to constitute a "living fossile" occurring in the course of evolution between the formation of the dimer and the gene duplication and fusion. The availability of the structure of the cytochrome c552-Pn and that of NiR from P. aeruginosa made it possible to identify putative surface patches at which the docking of c552to NiR-Pn may occur.
MAD structure of Pseudomonas nautica dimeric cytochrome c552 mimicks the c4 Dihemic cytochrome domain association.,Brown K, Nurizzo D, Besson S, Shepard W, Moura J, Moura I, Tegoni M, Cambillau C J Mol Biol. 1999 Jun 18;289(4):1017-28. PMID:10369779[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Brown K, Nurizzo D, Besson S, Shepard W, Moura J, Moura I, Tegoni M, Cambillau C. MAD structure of Pseudomonas nautica dimeric cytochrome c552 mimicks the c4 Dihemic cytochrome domain association. J Mol Biol. 1999 Jun 18;289(4):1017-28. PMID:10369779 doi:http://dx.doi.org/10.1006/jmbi.1999.2838
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