1jzj: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1jzj.gif|left|200px]]
- {{Structure
+==Pseudomonas aeruginosa Azurin Os(bpy)2(im)(His83)==
-|PDB= 1jzj |SIZE=350|CAPTION= <scene name='initialview01'>1jzj</scene>, resolution 1.80&Aring;
+<StructureSection load='1jzj' size='340' side='right'caption='[[1jzj]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <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=LOS:LAMBDA-BIS(2,2'-BIPYRIDINE)IMIDAZOLE+OSMIUM+(II)'>LOS</scene> and <scene name='pdbligand=IME:TETRA(IMIDAZOLE)DIAQUACOPPER (II)'>IME</scene>
+<table><tr><td colspan='2'>[[1jzj]] is a 2 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=1JZJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JZJ FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
-|GENE=
+<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=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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jzj OCA], [https://pdbe.org/1jzj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jzj RCSB], [https://www.ebi.ac.uk/pdbsum/1jzj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jzj 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/1jzj_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1jzj 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.
-'''Pseudomonas aeruginosa Azurin Os(bpy)2(im)(His83)'''
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1jzj" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-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.
+*[[Azurin 3D structures|Azurin 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-JZJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZJ OCA].
+__TOC__
+</StructureSection>
-==Reference==
+[[Category: Large Structures]]
-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://www.ncbi.nlm.nih.gov/pubmed/11716717 11716717]
 [[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: DOS]]
-[[Category: IME]]
-[[Category: LOS]]
-[[Category: blue-copper]]
-[[Category: electron transfer]]
-[[Category: osmium]]
-[[Category: tunneling]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:10:32 2008''