3o4c

<table><tr><td colspan='2'>[[3o4c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O4C OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3O4C FirstGlance]. <br>

</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=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jqz|1jqz]], [[3o3q|3o3q]], [[3o49|3o49]], [[3o4a|3o4a]], [[3o4b|3o4b]], [[3o4d|3o4d]], [[3o4e|3o4e]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3o4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o4c OCA], [http://pdbe.org/3o4c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3o4c RCSB], [http://www.ebi.ac.uk/pdbsum/3o4c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3o4c ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The majority of protein architectures exhibit elements of structural symmetry, and "gene duplication and fusion" is the evolutionary mechanism generally hypothesized to be responsible for their emergence from simple peptide motifs. Despite the central importance of the gene duplication and fusion hypothesis, experimental support for a plausible evolutionary pathway for a specific protein architecture has yet to be effectively demonstrated. To address this question, a unique "top-down symmetric deconstruction" strategy was utilized to successfully identify a simple peptide motif capable of recapitulating, via gene duplication and fusion processes, a symmetric protein architecture (the threefold symmetric beta-trefoil fold). The folding properties of intermediary forms in this deconstruction agree precisely with a previously proposed "conserved architecture" model for symmetric protein evolution. Furthermore, a route through foldable sequence-space between the simple peptide motif and extant protein fold is demonstrated. These results provide compelling experimental support for a plausible evolutionary pathway of symmetric protein architecture via gene duplication and fusion processes.

Experimental support for the evolution of symmetric protein architecture from a simple peptide motif.,Lee J, Blaber M Proc Natl Acad Sci U S A. 2011 Jan 4;108(1):126-30. Epub 2010 Dec 20. PMID:21173271<ref>PMID:21173271</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3o4c" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Synthetic construct sequences]]

[[Category: Blaber, M]]

[[Category: Lee, J]]

[[Category: De novo protein]]