1jzi: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Pseudomonas aeruginosa Azurin Re(phen)(CO)3(His83)== | ==Pseudomonas aeruginosa Azurin Re(phen)(CO)3(His83)== | ||
<StructureSection load='1jzi' size='340' side='right' caption='[[1jzi]], [[Resolution|resolution]] 1.62Å' scene=''> | <StructureSection load='1jzi' size='340' side='right' caption='[[1jzi]], [[Resolution|resolution]] 1.62Å' scene=''> | ||
| Line 5: | Line 6: | ||
</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=IME:TETRA(IMIDAZOLE)DIAQUACOPPER+(II)'>IME</scene>, <scene name='pdbligand=REP:(1,10+PHENANTHROLINE)-(TRI-CARBON+MONOXIDE)+RHENIUM+(I)'>REP</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=IME:TETRA(IMIDAZOLE)DIAQUACOPPER+(II)'>IME</scene>, <scene name='pdbligand=REP:(1,10+PHENANTHROLINE)-(TRI-CARBON+MONOXIDE)+RHENIUM+(I)'>REP</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]], [[1jzj|1jzj]]</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]], [[1jzj|1jzj]]</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=1jzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jzi OCA], [http://pdbe.org/1jzi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jzi RCSB], [http://www.ebi.ac.uk/pdbsum/1jzi 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=1jzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jzi OCA], [http://pdbe.org/1jzi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jzi RCSB], [http://www.ebi.ac.uk/pdbsum/1jzi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jzi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| Line 13: | Line 14: | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jz/1jzi_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jz/1jzi_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
| Line 28: | Line 29: | ||
</div> | </div> | ||
<div class="pdbe-citations 1jzi" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1jzi" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 12:01, 17 January 2018
Pseudomonas aeruginosa Azurin Re(phen)(CO)3(His83)Pseudomonas aeruginosa Azurin Re(phen)(CO)3(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 |
| ||||||||||||||||||