2lze: Difference between revisions

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lze OCA], [https://pdbe.org/2lze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lze RCSB], [https://www.ebi.ac.uk/pdbsum/2lze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lze ProSAT]</span></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=2lze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lze OCA], [https://pdbe.org/2lze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lze RCSB], [https://www.ebi.ac.uk/pdbsum/2lze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lze ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Engineering functional protein scaffolds capable of carrying out chemical catalysis is a major challenge in enzyme design. Starting from a noncatalytic protein scaffold, we recently generated a new RNA ligase by in vitro directed evolution. This artificial enzyme lost its original fold and adopted an entirely new structure with substantially enhanced conformational dynamics, demonstrating that a primordial fold with suitable flexibility is sufficient to carry out enzymatic function.
Structure and dynamics of a primordial catalytic fold generated by in vitro evolution.,Chao FA, Morelli A, Iii JC, Churchfield L, Hagmann LN, Shi L, Masterson LR, Sarangi R, Veglia G, Seelig B Nat Chem Biol. 2012 Dec 9. doi: 10.1038/nchembio.1138. PMID:23222886<ref>PMID:23222886</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2lze" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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