1etj

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<StructureSection load='1etj' size='340' side='right'caption='[[1etj]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='1etj' size='340' side='right'caption='[[1etj]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1etj]] is a 4 chain structure with sequence from [https://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=1ETJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ETJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1etj]] 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=1ETJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ETJ FirstGlance]. <br>
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</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></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<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></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=1etj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1etj OCA], [https://pdbe.org/1etj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1etj RCSB], [https://www.ebi.ac.uk/pdbsum/1etj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1etj ProSAT]</span></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=1etj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1etj OCA], [https://pdbe.org/1etj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1etj RCSB], [https://www.ebi.ac.uk/pdbsum/1etj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1etj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/AZUR_PSEAE AZUR_PSEAE]] Transfers electrons from cytochrome c551 to cytochrome oxidase.
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[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]]
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</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=1etj ConSurf].
</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=1etj ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The Met121Glu azurin mutant has been crystallized and the structure determined at a resolution of 2.3 A. In the crystal structure a carboxyl oxygen of Met121Glu is coordinated to the metal at a distance of 2.2 A. Single-crystal resonance Raman spectroscopy was used to show that the glutamic acid residue in the copper site was in the protonated state. Titration of this residue gives rise to a number of unusual, pH-dependent properties: as the pH is increased from 4 to 8, the S(Cys)-Cu ligand-to-metal charge transfer bands are blue shifted and their intensity ratio is reversed, the EPR signal changes from type 1 copper to a new form of protein-bound copper, and the redox potential changes from 370 to 180 mV. The spectroscopic changes in this pH interval are consistent with a two-state model. From the pH dependence of the optical and EPR spectra, pKa = 5.0 for the glutamic acid in the oxidized protein was determined.
 
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X-ray structure determination and characterization of the Pseudomonas aeruginosa azurin mutant Met121Glu.,Karlsson BG, Tsai LC, Nar H, Sanders-Loehr J, Bonander N, Langer V, Sjolin L Biochemistry. 1997 Apr 8;36(14):4089-95. PMID:9100002<ref>PMID:9100002</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1etj" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Azurin 3D structures|Azurin 3D structures]]
*[[Azurin 3D structures|Azurin 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bonander, N]]
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Karlsson, B G]]
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[[Category: Bonander N]]
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[[Category: Langer, V]]
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[[Category: Karlsson BG]]
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[[Category: Nar, H]]
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[[Category: Langer V]]
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[[Category: Sanders-Loehr, J]]
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[[Category: Nar H]]
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[[Category: Sjolin, L]]
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[[Category: Sanders-Loehr J]]
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[[Category: Tsai, L C]]
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[[Category: Sjolin L]]
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[[Category: Copper]]
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[[Category: Tsai L-C]]
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[[Category: Electron transport]]
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[[Category: Periplasmic]]
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Revision as of 10:06, 20 March 2024

AZURIN MUTANT WITH MET 121 REPLACED BY GLU

PDB ID 1etj

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