5e6g
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of De Novo Designed Protein CA01== | |
| + | <StructureSection load='5e6g' size='340' side='right' caption='[[5e6g]], [[Resolution|resolution]] 2.09Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5e6g]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E6G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E6G FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=5e6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e6g OCA], [http://pdbe.org/5e6g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e6g RCSB], [http://www.ebi.ac.uk/pdbsum/5e6g PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Natural recombination combines pieces of preexisting proteins to create new tertiary structures and functions. We describe a computational protocol, called SEWING, which is inspired by this process and builds new proteins from connected or disconnected pieces of existing structures. Helical proteins designed with SEWING contain structural features absent from other de novo designed proteins and, in some cases, remain folded at more than 100 degrees C. High-resolution structures of the designed proteins CA01 and DA05R1 were solved by x-ray crystallography (2.2 angstrom resolution) and nuclear magnetic resonance, respectively, and there was excellent agreement with the design models. This method provides a new strategy to rapidly create large numbers of diverse and designable protein scaffolds. | ||
| - | + | Design of structurally distinct proteins using strategies inspired by evolution.,Jacobs TM, Williams B, Williams T, Xu X, Eletsky A, Federizon JF, Szyperski T, Kuhlman B Science. 2016 May 6;352(6286):687-90. doi: 10.1126/science.aad8036. PMID:27151863<ref>PMID:27151863</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: Jacobs, T | + | <div class="pdbe-citations 5e6g" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Jacobs, T M]] | ||
[[Category: Kuhlman, B]] | [[Category: Kuhlman, B]] | ||
[[Category: Williams, T]] | [[Category: Williams, T]] | ||
| + | [[Category: Computational design]] | ||
| + | [[Category: De novo protein]] | ||
| + | [[Category: Protein engineering]] | ||
Revision as of 15:50, 1 June 2016
Crystal Structure of De Novo Designed Protein CA01
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