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| | ==Crystal structure of Re(phen)(CO)3 (Thr124His)(His83Gln) Azurin Cu(II) from Pseudomonas aeruginosa== | | ==Crystal structure of Re(phen)(CO)3 (Thr124His)(His83Gln) Azurin Cu(II) from Pseudomonas aeruginosa== |
| - | <StructureSection load='2i7s' size='340' side='right' caption='[[2i7s]], [[Resolution|resolution]] 1.35Å' scene=''> | + | <StructureSection load='2i7s' size='340' side='right'caption='[[2i7s]], [[Resolution|resolution]] 1.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2i7s]] is a 4 chain structure with sequence from [http://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=2I7S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2I7S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2i7s]] is a 4 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=2I7S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I7S FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CON:COBALT+TETRAAMMINE+ION'>CON</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=REP:(1,10+PHENANTHROLINE)-(TRI-CARBON+MONOXIDE)+RHENIUM+(I)'>REP</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">[[1bex|1bex]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CON:COBALT+TETRAAMMINE+ION'>CON</scene>, <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 ([http://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=2i7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i7s OCA], [https://pdbe.org/2i7s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i7s RCSB], [https://www.ebi.ac.uk/pdbsum/2i7s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i7s ProSAT]</span></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=2i7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i7s OCA], [http://pdbe.org/2i7s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2i7s RCSB], [http://www.ebi.ac.uk/pdbsum/2i7s PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|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/i7/2i7s_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i7/2i7s_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== |
| - | *[[Azurin|Azurin]] | + | *[[Azurin 3D structures|Azurin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Crane, B R]] | + | [[Category: Large Structures]] |
| - | [[Category: Gradinaru, C]] | + | [[Category: Pseudomonas aeruginosa]] |
| - | [[Category: Azurin]] | + | [[Category: Crane BR]] |
| - | [[Category: Electron transfer in protein]] | + | [[Category: Gradinaru C]] |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: Rhenium]]
| + | |
| Structural highlights
Function
AZUR_PSEAE Transfers electrons from cytochrome c551 to cytochrome oxidase.
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
Photoinduced relaxation processes of five structurally characterized Pseudomonas aeruginosa Re(I)(CO)(3)(alpha-diimine)(HisX) (X = 83, 107, 109, 124, 126)Cu(II) azurins have been investigated by time-resolved (ps-ns) IR spectroscopy and emission spectroscopy. Crystal structures reveal the presence of Re-azurin dimers and trimers that in two cases (X = 107, 124) involve van der Waals interactions between interdigitated diimine aromatic rings. Time-dependent emission anisotropy measurements confirm that the proteins aggregate in mM solutions (D(2)O, KP(i) buffer, pD = 7.1). Excited-state DFT calculations show that extensive charge redistribution in the Re(I)(CO)(3) --> diimine (3)MLCT state occurs: excitation of this (3)MLCT state triggers several relaxation processes in Re-azurins whose kinetics strongly depend on the location of the metallolabel on the protein surface. Relaxation is manifested by dynamic blue shifts of excited-state nu(CO) IR bands that occur with triexponential kinetics: intramolecular vibrational redistribution together with vibrational and solvent relaxation give rise to subps, approximately 2, and 8-20 ps components, while the approximately 10(2) ps kinetics are attributed to displacement (reorientation) of the Re(I)(CO)(3)(phen)(im) unit relative to the peptide chain, which optimizes Coulombic interactions of the Re(I) excited-state electron density with solvated peptide groups. Evidence also suggests that additional segmental movements of Re-bearing beta-strands occur without perturbing the reaction field or interactions with the peptide. Our work demonstrates that time-resolved IR spectroscopy and emission anisotropy of Re(I) carbonyl-diimine complexes are powerful probes of molecular dynamics at or around the surfaces of proteins and protein-protein interfacial regions.
Relaxation dynamics of Pseudomonas aeruginosa Re(I)(CO)3(alpha-diimine)(HisX)+ (X = 83, 107, 109, 124, 126)Cu(II) azurins.,Blanco-Rodriguez AM, Busby M, Ronayne K, Towrie M, Gradinaru C, Sudhamsu J, Sykora J, Hof M, Zalis S, Di Bilio AJ, Crane BR, Gray HB, Vlcek A Jr J Am Chem Soc. 2009 Aug 26;131(33):11788-800. PMID:19639996[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Blanco-Rodriguez AM, Busby M, Ronayne K, Towrie M, Gradinaru C, Sudhamsu J, Sykora J, Hof M, Zalis S, Di Bilio AJ, Crane BR, Gray HB, Vlcek A Jr. Relaxation dynamics of Pseudomonas aeruginosa Re(I)(CO)3(alpha-diimine)(HisX)+ (X = 83, 107, 109, 124, 126)Cu(II) azurins. J Am Chem Soc. 2009 Aug 26;131(33):11788-800. PMID:19639996 doi:10.1021/ja902744s
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