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6ldg
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the Zn-directed tetramer of the engineered cyt cb 562 variant, C96I AB5== | |
| + | <StructureSection load='6ldg' size='340' side='right'caption='[[6ldg]], [[Resolution|resolution]] 1.98Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6ldg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LDG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LDG 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]] 1.98Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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'>[https://proteopedia.org/fgij/fg.htm?mol=6ldg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ldg OCA], [https://pdbe.org/6ldg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ldg RCSB], [https://www.ebi.ac.uk/pdbsum/6ldg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ldg ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Directed evolution has provided us with great opportunities and prospects in the synthesis of tailor-made proteins. It, however, often requires at least mid to high throughput screening, necessitating more effective strategies for laboratory evolution. We herein demonstrate that protein symmetry can be a versatile criterion for searching for promising hotspots for the directed evolution of de novo oligomeric enzymes. The randomization of symmetry-related residues located at the rotational axes of artificial metallo-beta-lactamase yields drastic effects on catalytic activities, whereas that of non-symmetry-related, yet, proximal residues to the active site results in negligible perturbations. Structural and biochemical analysis of the positive hits indicates that seemingly trivial mutations at symmetry-related spots yield significant alterations in overall structures, metal-coordination geometry, and chemical environments of active sites. Our work implicates that numerous artificially designed and natural oligomeric proteins might have evolutionary advantages of propagating beneficial mutations using their global symmetry. | ||
| - | + | Symmetry-related residues as promising hotspots for the evolution of de novo oligomeric enzymes.,Yu J, Yang J, Seok C, Song WJ Chem Sci. 2021 Feb 17;12(14):5091-5101. doi: 10.1039/d0sc06823c. PMID:34168770<ref>PMID:34168770</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Song | + | <div class="pdbe-citations 6ldg" style="background-color:#fffaf0;"></div> |
| - | [[Category: Yu | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Song WJ]] | ||
| + | [[Category: Yu J]] | ||
Current revision
Crystal structure of the Zn-directed tetramer of the engineered cyt cb 562 variant, C96I AB5
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