6B87

Crystal structure of transmembrane protein TMHC2_E

Summary for 6B87

• Entry DOI: 10.2210/pdb6b87/pdb
• Descriptor: TMHC2_E (1 entity in total)
• Functional Keywords: de novo design, transmembrane protein, helical bundle, dimer, membrane protein
• Biological source: synthetic construct
• Total number of polymer chains: 4
• Total formula weight: 53175.51

Authors

Lu, P.,DiMaio, F.,Min, D.,Wei, K.Y.,Bowie, J.,Baker, D. (deposition date: 2017-10-05, release date: 2018-03-14, Last modification date: 2024-03-13)

Primary citation

Lu, P.,Min, D.,DiMaio, F.,Wei, K.Y.,Vahey, M.D.,Boyken, S.E.,Chen, Z.,Fallas, J.A.,Ueda, G.,Sheffler, W.,Mulligan, V.K.,Xu, W.,Bowie, J.U.,Baker, D.
Accurate computational design of multipass transmembrane proteins.
Science, 359:1042-1046, 2018

PubMed Abstract: The computational design of transmembrane proteins with more than one membrane-spanning region remains a major challenge. We report the design of transmembrane monomers, homodimers, trimers, and tetramers with 76 to 215 residue subunits containing two to four membrane-spanning regions and up to 860 total residues that adopt the target oligomerization state in detergent solution. The designed proteins localize to the plasma membrane in bacteria and in mammalian cells, and magnetic tweezer unfolding experiments in the membrane indicate that they are very stable. Crystal structures of the designed dimer and tetramer-a rocket-shaped structure with a wide cytoplasmic base that funnels into eight transmembrane helices-are very close to the design models. Our results pave the way for the design of multispan membrane proteins with new functions.

PubMed: 29496880
DOI: 10.1126/science.aaq1739

Experimental method

X-RAY DIFFRACTION (2.947 Å)