4qkt: Difference between revisions

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'''~~Unreleased~~ structure'''

==Azurin mutant M121EM44K with copper==

== 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>

</td></tr><tr><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><br>

<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qlw|4qlw]]</td></tr>

<tr><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://www.rcsb.org/pdb/explore.do?structureId=4qkt RCSB], [http://www.ebi.ac.uk/pdbsum/4qkt PDBsum]</span></td></tr>

<table>

== 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.

~~The entry 4qkt is ON HOLD until Paper Publication~~

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>

~~Authors~~: Liu, J., Robinson, H.~~, Lu, Y.~~

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

</div>

~~Description~~: ~~Azurin mutant M121EM44K with copper~~

== References ==

__TOC__

</StructureSection>

[[Category: Liu, J.]]

[[Category: Lu, Y.]]

[[Category: Robinson, H.]]

[[Category: Beta barrel]]

[[Category: Electron transport]]

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-'''Unreleased structure'''
+==Azurin mutant M121EM44K with copper==
+<StructureSection load='4qkt' size='340' side='right' caption='[[4qkt]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
+== 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>
+</td></tr><tr><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><br>
+<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qlw|4qlw]]</td></tr>
+<tr><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://www.rcsb.org/pdb/explore.do?structureId=4qkt RCSB], [http://www.ebi.ac.uk/pdbsum/4qkt PDBsum]</span></td></tr>
+<table>
+<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.
-The entry 4qkt is ON HOLD  until Paper Publication
+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>
-Authors: Liu, J., Robinson, H., Lu, Y.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Azurin mutant M121EM44K with copper
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Liu, J.]]
+[[Category: Lu, Y.]]
+[[Category: Robinson, H.]]
+[[Category: Beta barrel]]
+[[Category: Electron transport]]