4qlw: Difference between revisions
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New page: '''Unreleased structure''' The entry 4qlw is ON HOLD Authors: Liu, J., Robinson, H., Lu, Y. Description: AZURIN MUTANT M121E WITH IRON |
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==Azurin mutant M121E with iron== | |||
<StructureSection load='4qlw' size='340' side='right'caption='[[4qlw]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4qlw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QLW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QLW 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]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4qlw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qlw OCA], [https://pdbe.org/4qlw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qlw RCSB], [https://www.ebi.ac.uk/pdbsum/4qlw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qlw ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/AZUR_PSEAE AZUR_PSEAE] Transfers electrons from cytochrome c551 to cytochrome oxidase. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Much progress has been made in designing heme and dinuclear nonheme iron enzymes. In contrast, engineering mononuclear nonheme iron enzymes is lagging, even though these enzymes belong to a large class that catalyzes quite diverse reactions. Herein we report spectroscopic and X-ray crystallographic studies of Fe(II)-M121E azurin (Az), by replacing the axial Met121 and Cu(II) in wild type azurin (wtAz) with Glu and Fe(II), respectively. In contrast to the redox inactive Fe(II)-wtAz, the Fe(II)-M121EAz mutant can be readily oxidized by Na2IrCl6 and, interestingly, the protein exhib-its superoxide scavenging activity. Mossbauer and EPR spectroscopies, along with X-ray structural comparisons, revealed similarities and differences between Fe(II)-M121EAz, Fe(II)-wtAz, and superoxide reductase (SOR) and allowed design of the second generation mutant, Fe(II)-M121EM44KAz that exhibits increased superoxide scavenging activity, by two orders of magnitude. This finding demonstrates the importance of non-covalent secondary coordination sphere interactions in fine-tuning enzymatic activity. | |||
Redesigning the Blue Copper Azurin into a Redox-active Mononuclear Non-heme Iron Protein: Preparation and Study of Fe(II)-M121E Azurin.,Liu J, Meier K, Tian S, Zhang JL, Guo H, Schulz CE, Robinson H, Nilges MJ, Munck E, Lu Y J Am Chem Soc. 2014 Jul 31. PMID:25082811<ref>PMID:25082811</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4qlw" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Azurin 3D structures|Azurin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pseudomonas aeruginosa PAO1]] | |||
[[Category: Liu J]] | |||
[[Category: Lu Y]] | |||
[[Category: Robinson H]] | |||
