4qkt: Difference between revisions
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==Azurin mutant M121EM44K with copper== | ==Azurin mutant M121EM44K with copper== | ||
<StructureSection load='4qkt' size='340' side='right' caption='[[4qkt]], [[Resolution|resolution]] 1.64Å' scene=''> | <StructureSection load='4qkt' size='340' side='right'caption='[[4qkt]], [[Resolution|resolution]] 1.64Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4qkt]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QKT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QKT FirstGlance]. <br> | <table><tr><td colspan='2'>[[4qkt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QKT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QKT FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qlw|4qlw]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qlw|4qlw]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">azu, PA4922 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qkt OCA], [http://pdbe.org/4qkt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qkt RCSB], [http://www.ebi.ac.uk/pdbsum/4qkt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qkt ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qkt OCA], [http://pdbe.org/4qkt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qkt RCSB], [http://www.ebi.ac.uk/pdbsum/4qkt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qkt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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==See Also== | ==See Also== | ||
*[[Azurin|Azurin]] | *[[Azurin 3D structures|Azurin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Pseae]] | |||
[[Category: Liu, J]] | [[Category: Liu, J]] | ||
[[Category: Lu, Y]] | [[Category: Lu, Y]] | ||
Revision as of 11:55, 24 April 2019
Azurin mutant M121EM44K with copperAzurin mutant M121EM44K with copper
Structural highlights
Function[AZUR_PSEAE] Transfers electrons from cytochrome c551 to cytochrome oxidase. Publication Abstract from PubMedMuch 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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