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TitleMembrane protein solubilization and structure determination using de novo-designed proteins.
Journal, issue, pagesScience, Vol. 393, Issue 6806, Page eadr3817, Year 2026
Publish dateJul 2, 2026
AuthorsLjubica Mihaljević / David E Kim / Pooja D Bandawane / Helen E Eisenach / Andrew J Borst / Alexis Courbet / Connor Weidle / Kenneth D Carr / Everton Bettin / Qiushi Liu / Aldo T Trejos / Sagardip Majumder / Surabhi Kokane / Alexander Stevens / Edin Muratspahić / Thomas Schlichthaerle / Marc Expòsit / Xinting Li / Mila Lamb / Analisa Nicole Azcárraga Murray / Rashmi Ravichandran / Elizabeth C Williams / Shuyuan Hu / Lynda Stuart / Linda Grillová / Nicholas R Thomson / Michael Landreh / Pengxiang Chang / Lorenzo Giacani / Melissa J Caimano / Kelly L Hawley / Neil P King / David Baker /
PubMed AbstractDeveloping therapies and vaccines against integral membrane proteins is hindered by their extensive hydrophobic surfaces, which complicate production and structural analysis. Here, we describe a ...Developing therapies and vaccines against integral membrane proteins is hindered by their extensive hydrophobic surfaces, which complicate production and structural analysis. Here, we describe a general deep learning-based design approach for solubilizing native membrane proteins while preserving their sequence, fold, active-site, and ligand-binding properties. Genetically encoded de novo protein WRAPs [water-soluble RFdiffused amphipathic proteins] surround the lipid-interacting hydrophobic surfaces, rendering them thermostable and water-soluble without the need for detergents. We design WRAPs for both monomeric and oligomeric beta-barrel outer membrane proteins and helical multipass transmembrane proteins. A 2.95-angstrom-resolution cryo-electron microscopy structure of WRAPed mycobacterial porin demonstrates that WRAPs can be used for the structural determination of membrane proteins in solution. As a step toward syphilis vaccine development, we generated soluble versions of antigens.
External linksScience / PubMed:42391386
MethodsEM (single particle)
Resolution3.9 - 4.88 Å
Structure data

EMDB-75290: cryoEM map for soluble OmpA beta-barrel WRAPs
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-75291: cryoEM map of OmpA helical WRAP
Method: EM (single particle) / Resolution: 4.88 Å

EMDB-75346: Membrane protein solubilization and structure determination using de novo-designed amphipathic proteins
Method: EM (single particle) / Resolution: 4.74 Å

EMDB-75350: WRAP-TP0698
Method: EM (single particle) / Resolution: 4.01 Å

Source
  • E coli (bacteria)
  • synthetic construct (others)

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