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[[Image:1etj.gif|left|200px]]
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{{STRUCTURE_1etj|  PDB=1etj  |  SCENE=  }}
'''AZURIN MUTANT WITH MET 121 REPLACED BY GLU'''


==AZURIN MUTANT WITH MET 121 REPLACED BY GLU==
<StructureSection load='1etj' size='340' side='right'caption='[[1etj]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
</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/et/1etj_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=1etj ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1ETJ 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=1ETJ OCA].
</div>
<div class="pdbe-citations 1etj" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/9100002 9100002]
*[[Azurin 3D structures|Azurin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Single protein]]
[[Category: Bonander N]]
[[Category: Bonander, N.]]
[[Category: Karlsson BG]]
[[Category: Karlsson, B G.]]
[[Category: Langer V]]
[[Category: Langer, V.]]
[[Category: Nar H]]
[[Category: Nar, H.]]
[[Category: Sanders-Loehr J]]
[[Category: Sanders-Loehr, J.]]
[[Category: Sjolin L]]
[[Category: Sjolin, L.]]
[[Category: Tsai L-C]]
[[Category: Tsai, L C.]]
[[Category: Copper]]
[[Category: Electron transport]]
[[Category: Periplasmic]]
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Retrieved from "https://proteopedia.org/1etj"