3q7y
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal structure of K15R/E18D/Y22W/H41G/F44W/E51D/E53P/K57R/E60D/Y64W/H82G/F85W/E90D/E94P/K98R/E101D/Y108W/H129G/F132W/E137D Symfoil-4P: de novo designed beta-trefoil architecture with symmetric primary structure== | |
| - | + | <StructureSection load='3q7y' size='340' side='right' caption='[[3q7y]], [[Resolution|resolution]] 1.45Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3q7y]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q7Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q7Y FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jqz|1jqz]], [[3o4d|3o4d]], [[3q7w|3q7w]], [[3q7x|3q7x]]</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=3q7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q7y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q7y RCSB], [http://www.ebi.ac.uk/pdbsum/3q7y PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A compendium of different types of abiotic chemical syntheses identifies a consensus set of 10 "prebiotic" alpha-amino acids. Before the emergence of biosynthetic pathways, this set is the most plausible resource for protein formation (i.e., proteogenesis) within the overall process of abiogenesis. An essential unsolved question regarding this prebiotic set is whether it defines a "foldable set"-that is, does it contain sufficient chemical information to permit cooperatively folding polypeptides? If so, what (if any) characteristic properties might such polypeptides exhibit? To investigate these questions, two "primitive" versions of an extant protein fold (the beta-trefoil) were produced by top-down symmetric deconstruction, resulting in a reduced alphabet size of 12 or 13 amino acids and a percentage of prebiotic amino acids approaching 80%. These proteins show a substantial acidification of pI and require high salt concentrations for cooperative folding. The results suggest that the prebiotic amino acids do comprise a foldable set within the halophile environment. | ||
| - | + | Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein.,M Longo L, Lee J, Blaber M Proc Natl Acad Sci U S A. 2013 Jan 22. PMID:23341608<ref>PMID:23341608</ref> | |
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| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: Blaber, M | + | == References == |
| - | [[Category: Lee, J | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Blaber, M]] | ||
| + | [[Category: Lee, J]] | ||
[[Category: Beta-trefoil]] | [[Category: Beta-trefoil]] | ||
[[Category: De novo protein]] | [[Category: De novo protein]] | ||
Revision as of 16:43, 21 December 2014
Crystal structure of K15R/E18D/Y22W/H41G/F44W/E51D/E53P/K57R/E60D/Y64W/H82G/F85W/E90D/E94P/K98R/E101D/Y108W/H129G/F132W/E137D Symfoil-4P: de novo designed beta-trefoil architecture with symmetric primary structure
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