Abstract:
:The urea channel of Helicobacterpylori (HpUreI) is an ideal drug target for preventing gastric cancer but incomplete understanding of its gating mechanism has hampered development of inhibitors for the eradication of H. pylori. Here, we present the cryo-EM structures of HpUreI in closed and open conformations, both at a resolution of 2.7 Å. Our hexameric structures of this small membrane protein (~21 kDa/protomer) resolve its periplasmic loops and carboxyl terminus that close and open the channel, and define a gating mechanism that is pH dependent and requires cooperativity between protomers in the hexamer. Gating is further associated with well-resolved changes in the channel-lining residues that modify the shape and length of the urea pore. Site-specific mutations in the periplasmic domain and urea pore identified key residues important for channel function. Drugs blocking the urea pore based on our structures should lead to a new strategy for H. pylori eradication.
journal_name
Sci Advjournal_title
Science advancesauthors
Cui Y,Zhou K,Strugatsky D,Wen Y,Sachs G,Zhou ZH,Munson Kdoi
10.1126/sciadv.aav8423subject
Has Abstractpub_date
2019-03-20 00:00:00pages
eaav8423issue
3issn
2375-2548pii
aav8423journal_volume
5pub_type
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