View source for 8bct


==X-ray crystal structure of a de novo selected helix-loop-helix heterodimer in a syn arrangement, 26alpha/26beta==
<StructureSection load='8bct' size='340' side='right'caption='[[8bct]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8bct]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BCT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BCT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=8bct FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bct OCA], [https://pdbe.org/8bct PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bct RCSB], [https://www.ebi.ac.uk/pdbsum/8bct PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bct ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Synthetic biology applications would benefit from protein modules of reduced complexity that function orthogonally to cellular components. As many subcellular processes depend on peptide-protein or protein-protein interactions, de novo designed polypeptides that can bring together other proteins controllably are particularly useful. Thanks to established sequence-to-structure relationships, helical bundles provide good starting points for such designs. Typically, however, such designs are tested in vitro and function in cells is not guaranteed. Here, we describe the design, characterization, and application of de novo helical hairpins that heterodimerize to form 4-helix bundles in cells. Starting from a rationally designed homodimer, we construct a library of helical hairpins and identify complementary pairs using bimolecular fluorescence complementation in E. coli. We characterize some of the pairs using biophysics and X-ray crystallography to confirm heterodimeric 4-helix bundles. Finally, we demonstrate the function of an exemplar pair in regulating transcription in both E. coli and mammalian cells.

Design and Selection of Heterodimerizing Helical Hairpins for Synthetic Biology.,Smith AJ, Naudin EA, Edgell CL, Baker EG, Mylemans B, FitzPatrick L, Herman A, Rice HM, Andrews DM, Tigue N, Woolfson DN, Savery NJ ACS Synth Biol. 2023 Jun 16;12(6):1845-1858. doi: 10.1021/acssynbio.3c00231. Epub , 2023 May 24. PMID:37224449<ref>PMID:37224449</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8bct" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Mylemans B]]
[[Category: Naudin EA]]
[[Category: Savery NJ]]
[[Category: Smith AJ]]
[[Category: Woolfson DN]]