View source for 4p5r


==Structure of oxidized W45Y mutant of amicyanin==
<StructureSection load='4p5r' size='340' side='right'caption='[[4p5r]], [[Resolution|resolution]] 1.09&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4p5r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P5R 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]] 1.09&#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=NA:SODIUM+ION'>NA</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=4p5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p5r OCA], [https://pdbe.org/4p5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p5r RCSB], [https://www.ebi.ac.uk/pdbsum/4p5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p5r ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AMCY_PARDE AMCY_PARDE] Primary acceptor of electrons from methylamine dehydrogenase. Passes those electrons on either a soluble cytochrome c or to pseudoazurin.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The cupredoxin amicyanin possesses a single tryptophan residue, Trp45. Its fluorescence is quenched when copper is bound even though it separated by 10.1A. Mutation of Trp45 to Ala, Phe, Leu and Lys resulted in undetectable protein expression. A W45Y amicyanin variant was isolated. The W45Y mutation did not alter the spectroscopic properties or intrinsic redox potential of amicyanin, but increased the pKa value for the pH-dependent redox potential by 0.5units. This is due to a hydrogen-bond involving the His95 copper ligand which is present in reduced W45Y amicyanin but not in native amicyanin. The W45Y mutation significantly decreased the thermal stability of amicyanin, as determined by changes in the visible absorbance of oxidized amicyanin and in the circular dichroism spectra for oxidized, reduced and apo forms of amicyanin. Comparison of the crystal structures suggests that the decreased stability of W45Y amicyanin may be attributed to the loss of a strong interior hydrogen bond between Trp45 and Tyr90 in native amicyanin which links two of the beta-sheets that comprise the overall structure of amicyanin. Thus, Trp45 is critical for stabilizing the structure of amicyanin but it does not influence the electronic properties of the copper which quenches its fluorescence.

The sole tryptophan of amicyanin enhances its thermal stability but does not influence the electronic properties of the type 1 copper site.,Dow BA, Sukumar N, Matos JO, Choi M, Schulte A, Tatulian SA, Davidson VL Arch Biochem Biophys. 2014 Apr 1. pii: S0003-9861(14)00111-8. doi:, 10.1016/j.abb.2014.03.010. PMID:24704124<ref>PMID:24704124</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4p5r" style="background-color:#fffaf0;"></div>

==See Also==
*[[Amicyanin 3D structures|Amicyanin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Paracoccus denitrificans]]
[[Category: Davidson VL]]
[[Category: Sukumar N]]