6dsl

<StructureSection load='6dsl' size='340' side='right'caption='[[6dsl]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[6dsl]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt7 Bpt7]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DSL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DSL FirstGlance]. <br>

</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=6dsl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dsl OCA], [http://pdbe.org/6dsl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dsl RCSB], [http://www.ebi.ac.uk/pdbsum/6dsl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dsl ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Split inteins associate to trigger protein splicing in trans, a post-translational modification in which protein sequences fused to the intein pair are ligated together in a traceless manner. Recently, a family of naturally split inteins has been identified that is split at a noncanonical location in the primary sequence. These atypically split inteins show considerable promise in protein engineering applications; however, the mechanism by which they associate is unclear and must be different from that of previously characterized canonically split inteins due to unique topological restrictions. Here, we use a consensus design strategy to generate an atypical split intein pair (Cat) that has greatly improved activity and is amenable to detailed biochemical and biophysical analysis. Guided by the solution structure of Cat, we show that the association of the fragments involves a disorder-to-order structural transition driven by hydrophobic interactions. This molecular recognition mechanism satisfies the topological constraints of the intein fold and, importantly, ensures that premature chemistry does not occur prior to fragment complementation. Our data lead a common blueprint for split intein complementation in which localized structural rearrangements are used to drive folding and regulate protein-splicing activity.

An Atypical Mechanism of Split Intein Molecular Recognition and Folding.,Stevens AJ, Sekar G, Gramespacher JA, Cowburn D, Muir TW J Am Chem Soc. 2018 Sep 10. doi: 10.1021/jacs.8b07334. PMID:30156841<ref>PMID:30156841</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 6dsl" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bpt7]]

[[Category: Cowburn, D]]

[[Category: Muir, T W]]

[[Category: Sekar, G]]

[[Category: Stevens, A J]]

[[Category: Trans splicing]]