6h5h
From Proteopedia
(Difference between revisions)
| (4 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==A computationally designed dRP lyase domain reconstructed from two heterologous fragments== | |
| + | <StructureSection load='6h5h' size='340' side='right'caption='[[6h5h]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6h5h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H5H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6H5H FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=6h5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h5h OCA], [https://pdbe.org/6h5h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6h5h RCSB], [https://www.ebi.ac.uk/pdbsum/6h5h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6h5h ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Computational design with supersecondary structures as building blocks has proven effective in the construction of new proteins with controlled geometries. So far, this approach has primarily exploited amplification, effectively harnessing the internal folding propensity of self-compatible fragments to achieve sufficient enthalpy for folding. Here we exploit an interface-driven strategy to depart from the repeat design realm, constructing an asymmetric, globular domain from heterologous supersecondary structures. We report the successful design of a dRP lyase domain fold, which agrees with the experimental NMR structure at atomic accuracy (backbone RMSD of 0.94A). Our results show that the residual folding information within conserved fragments, combined with efficient interface-directed sampling, can effectively yield globular proteins with novel sequences and biophysical properties. | ||
| - | + | Asymmetric protein design from conserved supersecondary structures.,ElGamacy M, Coles M, Lupas A J Struct Biol. 2018 Dec;204(3):380-387. doi: 10.1016/j.jsb.2018.10.010. Epub 2018, Oct 26. PMID:30558718<ref>PMID:30558718</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Coles | + | <div class="pdbe-citations 6h5h" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Coles M]] | ||
| + | [[Category: ElGamacy M]] | ||
| + | [[Category: Lupas AN]] | ||
Current revision
A computationally designed dRP lyase domain reconstructed from two heterologous fragments
| |||||||||||
