Studying macromolecular structures by Cryo-EM

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  • Writer 최고관리자
  • 2017-09-12



▶Subject: Studying macromolecular structures by Cryo-EM

▶Speaker: Roh, Soung-Hun, Ph.D. (Stanford University)
▶Date: 2:00PM/Sep. 15(Fri.)/2017
▶Place: Life Science Bldg. #104
▶Inquiry:Prof. Yunje Cho (279-2288)
The molecular mechanism of transmembrane proton translocation in rotary motor ATPases is not fully understood. Here we report the 3.5 Å resolution cryoEM structure of the lipid nanodisc-reconstituted Vo proton channel of the yeast vacuolar H+-ATPase (V-ATPase), captured in a physiologically relevant, autoinhibited state. The resulting atomic model provides unprecedented detail for the amino acid residues at the interface of the proteolipid ring and the transmembrane portion of subunit a that constitute the proton pathway. Together with previous mutagenesis studies, we propose the chemical basis of transmembrane proton transport. Moreover, we discovered that the C-terminus of the assembly factor Voa1 is an integral component of mature Vo. Voa1’s C-terminal transmembrane α helix is bound inside the proteolipid ring, where it contributes to the stability of the complex. Our structure rationalizes possible mechanisms by which mutations in human Vo can result in disease phenotypes, and may thus provide new avenues for therapeutic interventions

* This seminar will be given in English.
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