5o94: Difference between revisions

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'''Unreleased structure'''


The entry 5o94 is ON HOLD  until Paper Publication
==X-ray structure of a zinc binding GB1 mutant==
<StructureSection load='5o94' size='340' side='right' caption='[[5o94]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5o94]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O94 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5O94 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5o94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o94 OCA], [http://pdbe.org/5o94 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o94 RCSB], [http://www.ebi.ac.uk/pdbsum/5o94 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o94 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The development of thermostable and solvent-tolerant metalloproteins is a long-sought goal for many applications in synthetic biology and biotechnology. In this work, we were able to engineer a highly thermostable and organic solvent-stable metallo variant of the B1 domain of protein G (GB1) with a tetrahedral zinc binding site reminiscent of the one of thermolysin. Promising candidates were designed computationally by applying a protocol based on classical and first-principles molecular dynamics simulations in combination with genetic algorithm optimization. The most promising of the computationally predicted mutants was expressed and structurally characterized and yielded a highly thermostable protein. The experimental results thus confirm the predictive power of the applied computational protein engineering approach for the de novo design of highly stable metalloproteins.


Authors: Rothlisberger, U., Bozkurt, E., Hovius, R., Perez, M.A.S., Browning, N.J.
Genetic Algorithm Based Design and Experimental Characterization of a Highly Thermostable Metalloprotein.,Bozkurt E, Perez MAS, Hovius R, Browning NJ, Rothlisberger U J Am Chem Soc. 2018 Mar 26. doi: 10.1021/jacs.7b10660. PMID:29336153<ref>PMID:29336153</ref>


Description: X-ray structure of a zinc binding GB1 mutant
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Perez, M.A.S]]
<div class="pdbe-citations 5o94" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bozkurt, E]]
[[Category: Bozkurt, E]]
[[Category: Browning, N.J]]
[[Category: Browning, N J]]
[[Category: Hovius, R]]
[[Category: Hovius, R]]
[[Category: Perez, M A.S]]
[[Category: Rothlisberger, U]]
[[Category: Rothlisberger, U]]
[[Category: Immunoglobulin bindi]]
[[Category: Metal binding protein]]
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