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| | <StructureSection load='3n2j' size='340' side='right'caption='[[3n2j]], [[Resolution|resolution]] 1.35Å' scene=''> | | <StructureSection load='3n2j' size='340' side='right'caption='[[3n2j]], [[Resolution|resolution]] 1.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3n2j]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N2J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N2J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3n2j]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N2J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N2J 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></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]] 1.35Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4azu|4azu]]</div></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></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">azu, PA4922 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</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=3n2j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n2j OCA], [https://pdbe.org/3n2j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n2j RCSB], [https://www.ebi.ac.uk/pdbsum/3n2j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n2j 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=3n2j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n2j OCA], [https://pdbe.org/3n2j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n2j RCSB], [https://www.ebi.ac.uk/pdbsum/3n2j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n2j ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/AZUR_PSEAE AZUR_PSEAE]] Transfers electrons from cytochrome c551 to cytochrome oxidase.
| + | [https://www.uniprot.org/uniprot/AZUR_PSEAE AZUR_PSEAE] Transfers electrons from cytochrome c551 to cytochrome oxidase. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Alagaratnam, S]] | + | [[Category: Pseudomonas aeruginosa]] |
| - | [[Category: Canters, G W]] | + | [[Category: Alagaratnam S]] |
| - | [[Category: Einsle, O]] | + | [[Category: Canters GW]] |
| - | [[Category: Hoffmann, M]] | + | [[Category: Einsle O]] |
| - | [[Category: Copper protein]]
| + | [[Category: Hoffmann M]] |
| - | [[Category: Electron transfer]]
| + | |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: Pseudo-translation]]
| + | |
| Structural highlights
Function
AZUR_PSEAE Transfers electrons from cytochrome c551 to cytochrome oxidase.
Publication Abstract from PubMed
The reactivity of a variant of the blue copper protein, azurin from Pseudomonas aeruginosa, was investigated with laser flash photolysis and compared with the reactivity of the wild-type (WT) protein. The variant was obtained by changing the Cu ligating His117 for a glycine. The mutation creates a gap in the ligand shell of the Cu that can be filled with external ligands or water molecules. The crystal structure of the H117G variant is reported. It shows that the immediate surrounding of the Cu site in the variant exhibits less rigidity than in the WT protein and that the loop containing the Cu ligands Cys112, His117 and Met121 in the WT protein has gained flexibility in the H117G variant. Flash photolysis experiments were performed with 5-deazariboflavin and 8alpha-imidazolyl-(N-propylyl)-amino riboflavin as electron donors to probe the reactivity of WT and H117G azurin, and of H117G azurin for which the gap in the Cu co-ordination shell was filled with imidazole. 8alpha-Imidazolyl-(N-propylyl)-amino riboflavin appears one to two orders less efficient as a photo-flash reductant than 5-deazariboflavin. The reactivity of the H117G variant in the absence of external ligands appears to be 2.5-fold lower than the WT reactivity (second-order rate constants of 51 +/- 2 x 10(7) m(-1) .s(-1) versus 21 +/- 1 x 10(7) m(-1) .s(-1) ), whereas the addition of imidazole restores reactivity to above the WT level (71 +/- 4 x 10(7) m(-1) .s(-1) ). The differences are discussed in terms of structural modifications and changes in reorganizational energy and electronic coupling. Database Structural data are available in the Protein Data Bank under the accession number 3N2J. Structured digital abstract * Azurin binds to Azurin by x-ray crystallography (View interaction).
Probing the reactivity of different forms of azurin by flavin photoreduction.,Alagaratnam S, Meeuwenoord NJ, Navarro JA, Hervas M, De la Rosa MA, Hoffmann M, Einsle O, Ubbink M, Canters GW FEBS J. 2011 Feb 26. doi: 10.1111/j.1742-4658.2011.08067.x. PMID:21352498[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Alagaratnam S, Meeuwenoord NJ, Navarro JA, Hervas M, De la Rosa MA, Hoffmann M, Einsle O, Ubbink M, Canters GW. Probing the reactivity of different forms of azurin by flavin photoreduction. FEBS J. 2011 Feb 26. doi: 10.1111/j.1742-4658.2011.08067.x. PMID:21352498 doi:10.1111/j.1742-4658.2011.08067.x
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