1jze: Difference between revisions

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-[[Image:1jze.gif|left|200px]]<br /><applet load="1jze" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1jze, resolution 1.60&Aring;" />
-'''Pseudomonas aeruginosa Azurin Ru(bpy)2(im)(His83)'''<br />
-==Overview==
+==Pseudomonas aeruginosa Azurin Ru(bpy)2(im)(His83)==
-Rates 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) --&gt; 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.
+<StructureSection load='1jze' size='340' side='right'caption='[[1jze]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1jze]] is a 1 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=1JZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JZE FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</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>, <scene name='pdbligand=DRU:DELTA-BIS(2,2-BIPYRIDINE)IMIDAZOLE+RUTHENIUM+(II)'>DRU</scene>, <scene name='pdbligand=LRU:LAMBDA-BIS(2,2-BIPYRIDINE)IMIDAZOLE+RUTHENIUM+(II)'>LRU</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=1jze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jze OCA], [https://pdbe.org/1jze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jze RCSB], [https://www.ebi.ac.uk/pdbsum/1jze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jze ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/AZUR_PSEAE AZUR_PSEAE] Transfers electrons from cytochrome c551 to cytochrome oxidase.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jz/1jze_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </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/main_output.php?pdb_ID=1jze ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Rates 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) --&gt; 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.
-==About this Structure==
+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<ref>PMID:11716717</ref>
-JZE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with CU, DRU and LRU as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JZE OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11716717 11716717]
+</div>
+<div class="pdbe-citations 1jze" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Azurin 3D structures|Azurin 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Pseudomonas aeruginosa]]
-[[Category: Single protein]]
+[[Category: Crane BR]]
-[[Category: Bilio, A.J.Di.]]
+[[Category: Di Bilio AJ]]
-[[Category: Crane, B.R.]]
+[[Category: Gray HB]]
-[[Category: Gray, H.B.]]
+[[Category: Winkler JR]]
-[[Category: Winkler, J.R.]]
-[[Category: CU]]
-[[Category: DRU]]
-[[Category: LRU]]
-[[Category: blue-copper]]
-[[Category: electron transfer]]
-[[Category: ruthenium]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:43:04 2007''