1gr7

<table><tr><td colspan='2'>[[1gr7]] 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=1GR7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GR7 FirstGlance]. <br>

</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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ag0|1ag0]], [[1azn|1azn]], [[1azr|1azr]], [[1azu|1azu]], [[1bex|1bex]], [[1cc3|1cc3]], [[1e5y|1e5y]], [[1e5z|1e5z]], [[1e65|1e65]], [[1e67|1e67]], [[1etj|1etj]], [[1ezl|1ezl]], [[1i53|1i53]], [[1ils|1ils]], [[1ilu|1ilu]], [[1jze|1jze]], [[1jzf|1jzf]], [[1jzg|1jzg]], [[1jzh|1jzh]], [[1jzi|1jzi]], [[1jzj|1jzj]], [[1nzr|1nzr]], [[1vlx|1vlx]], [[2azu|2azu]], [[2tsa|2tsa]], [[2tsb|2tsb]], [[3azu|3azu]], [[4azu|4azu]], [[5azu|5azu]]</div></td></tr>

[[https://www.uniprot.org/uniprot/AZUR_PSEAE AZUR_PSEAE]] Transfers electrons from cytochrome c551 to cytochrome oxidase.

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== Publication Abstract from PubMed ==

Azurin is a cupredoxin, which functions as an electron carrier. Its fold is dominated by a beta-sheet structure. In the present study, azurin serves as a model system to investigate the importance of a conserved disulphide bond for protein stability and folding/unfolding. For this purpose, we have examined two azurin mutants, the single mutant Cys3Ser, which disrupts azurin's conserved disulphide bond, and the double mutant Cys3Ser/Ser100Pro, which contains an additional mutation at a site distant from the conserved disulphide. The crystal structure of the azurin double mutant has been determined to 1.8 A resolution(2), with a crystallographic R-factor of 17.5% (R(free)=20.8%). A comparison with the wild-type structure reveals that structural differences are limited to the sites of the mutations. Also, the rates of folding and unfolding as determined by CD and fluorescence spectroscopy are almost unchanged. The main difference to wild-type azurin is a destabilisation by approximately 20 kJ x mol(-1), constituting half the total folding energy of the wild-type protein. Thus, the disulphide bond constitutes a vital component in giving azurin its stable fold.

Crystal structure of the double azurin mutant Cys3Ser/Ser100Pro from Pseudomonas aeruginosa at 1.8 A resolution: its folding-unfolding energy and unfolding kinetics.,Okvist M, Bonander N, Sandberg A, Karlsson BG, Krengel U, Xue Y, Sjolin L Biochim Biophys Acta. 2002 Apr 29;1596(2):336-45. PMID:12007613<ref>PMID:12007613</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1gr7" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bonander, N]]

[[Category: Karlsson, B G]]

[[Category: Krengel, U]]

[[Category: Okvist, M]]

[[Category: Sandberg, A]]

[[Category: Sjolin, L]]

[[Category: Xue, Y]]

[[Category: Electron transport]]