View source for 9bei


==Cryo-EM structure of synthetic claudin-4 complex with Clostridium perfringens enterotoxin C-terminal domain, sFab COP-2, and Nanobody==
<StructureSection load='9bei' size='340' side='right'caption='[[9bei]], [[Resolution|resolution]] 4.16&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9bei]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens], [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9BEI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9BEI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.16&#8491;</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=9bei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9bei OCA], [https://pdbe.org/9bei PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9bei RCSB], [https://www.ebi.ac.uk/pdbsum/9bei PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9bei ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ELTB_CLOPF ELTB_CLOPF] This enterotoxin is responsible for many cases of a mild type of food poisoning.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
De novo design of complex protein folds using solely computational means remains a substantial challenge(1). Here we use a robust deep learning pipeline to design complex folds and soluble analogues of integral membrane proteins. Unique membrane topologies, such as those from G-protein-coupled receptors(2), are not found in the soluble proteome, and we demonstrate that their structural features can be recapitulated in solution. Biophysical analyses demonstrate the high thermal stability of the designs, and experimental structures show remarkable design accuracy. The soluble analogues were functionalized with native structural motifs, as a proof of concept for bringing membrane protein functions to the soluble proteome, potentially enabling new approaches in drug discovery. In summary, we have designed complex protein topologies and enriched them with functionalities from membrane proteins, with high experimental success rates, leading to a de facto expansion of the functional soluble fold space.

Computational design of soluble and functional membrane protein analogues.,Goverde CA, Pacesa M, Goldbach N, Dornfeld LJ, Balbi PEM, Georgeon S, Rosset S, Kapoor S, Choudhury J, Dauparas J, Schellhaas C, Kozlov S, Baker D, Ovchinnikov S, Vecchio AJ, Correia BE Nature. 2024 Jun 19. doi: 10.1038/s41586-024-07601-y. PMID:38898281<ref>PMID:38898281</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9bei" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Clostridium perfringens]]
[[Category: Escherichia coli]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Vecchio AJ]]