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==Pseudomonas aeruginosa Azurin Os(bpy)2(im)(His83)== | ==Pseudomonas aeruginosa Azurin Os(bpy)2(im)(His83)== | ||
<StructureSection load='1jzj' size='340' side='right' caption='[[1jzj]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1jzj' size='340' side='right' caption='[[1jzj]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=DOS:DELTA-BIS(2,2-BIPYRIDINE)IMIDAZOLE+OSMIUM+(II)'>DOS</scene>, <scene name='pdbligand=IME:TETRA(IMIDAZOLE)DIAQUACOPPER+(II)'>IME</scene>, <scene name='pdbligand=LOS:LAMBDA-BIS(2,2-BIPYRIDINE)IMIDAZOLE+OSMIUM+(II)'>LOS</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=DOS:DELTA-BIS(2,2-BIPYRIDINE)IMIDAZOLE+OSMIUM+(II)'>DOS</scene>, <scene name='pdbligand=IME:TETRA(IMIDAZOLE)DIAQUACOPPER+(II)'>IME</scene>, <scene name='pdbligand=LOS:LAMBDA-BIS(2,2-BIPYRIDINE)IMIDAZOLE+OSMIUM+(II)'>LOS</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jze|1jze]], [[1jzf|1jzf]], [[1jzg|1jzg]], [[1jzh|1jzh]], [[1jzi|1jzi]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jze|1jze]], [[1jzf|1jzf]], [[1jzg|1jzg]], [[1jzh|1jzh]], [[1jzi|1jzi]]</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=1jzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jzj OCA], [http://pdbe.org/1jzj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jzj RCSB], [http://www.ebi.ac.uk/pdbsum/1jzj PDBsum]</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=1jzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jzj OCA], [http://pdbe.org/1jzj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jzj RCSB], [http://www.ebi.ac.uk/pdbsum/1jzj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jzj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jzj ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1jzj" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1jzj" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:19, 11 October 2017
Pseudomonas aeruginosa Azurin Os(bpy)2(im)(His83)Pseudomonas aeruginosa Azurin Os(bpy)2(im)(His83)
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 PubMedRates of reduction of Os(III), Ru(III), and Re(I) by Cu(I) in His83-modified Pseudomonas aeruginosa azurins (M-Cu distance approximately 17 A) have been measured in single crystals, where protein conformation and surface solvation are precisely defined by high-resolution X-ray structure determinations: 1.7(8) x 10(6) s(-1) (298 K), 1.8(8) x 10(6) s(-1) (140 K), [Ru(bpy)2(im)(3+)-]; 3.0(15) x 10(6) s(-1) (298 K), [Ru(tpy)(bpy)(3+)-]; 3.0(15) x 10(6) s(-1) (298 K), [Ru(tpy)(phen)(3+)-]; 9.0(50) x 10(2) s(-1) (298 K), [Os(bpy)2(im)(3+)-]; 4.4(20) x 10(6) s(-1) (298 K), [Re(CO)3(phen)(+)] (bpy = 2,2'-bipyridine; im = imidazole; tpy = 2,2':6',2' '-terpyridine; phen = 1,10-phenanthroline). The time constants for electron tunneling in crystals are roughly the same as those measured in solution, indicating very similar protein structures in the two states. High-resolution structures of the oxidized (1.5 A) and reduced (1.4 A) states of Ru(II)(tpy)(phen)(His83)Az establish that very small changes in copper coordination accompany reduction but reveal a shorter axial interaction between copper and the Gly45 peptide carbonyl oxygen [2.6 A for Cu(II)] than had been recognized previously. Although Ru(bpy)2(im)(His83)Az is less solvated in the crystal, the reorganization energy for Cu(I) --> Ru(III) electron transfer falls in the range (0.6-0.8 eV) determined experimentally for the reaction in solution. Our work suggests that outer-sphere protein reorganization is the dominant activation component required for electron tunneling. Electron tunneling in single crystals of Pseudomonas aeruginosa azurins.,Crane BR, Di Bilio AJ, Winkler JR, Gray HB J Am Chem Soc. 2001 Nov 28;123(47):11623-31. PMID:11716717[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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