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TitlepH-dependent gating mechanism of the urea channel revealed by cryo-EM.
Journal, issue, pagesSci Adv, Vol. 5, Issue 3, Page eaav8423, Year 2019
Publish dateMar 20, 2019
AuthorsYanxiang Cui / Kang Zhou / David Strugatsky / Yi Wen / George Sachs / Z Hong Zhou / Keith Munson /
PubMed AbstractThe urea channel of (UreI) 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 . ...The urea channel of (UreI) 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 . Here, we present the cryo-EM structures of UreI 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 eradication.
External linksSci Adv / PubMed:30906870 / PubMed Central
MethodsEM (single particle)
Resolution2.7 Å
Structure data

0498

6nsj

EMDB-0498, PDB-6nsj:
CryoEM structure of Helicobacter pylori urea channel in closed state
Method: EM (single particle) / Resolution: 2.7 Å

0499

6nsk

EMDB-0499, PDB-6nsk:
CryoEM structure of Helicobacter pylori urea channel in open state.
Method: EM (single particle) / Resolution: 2.7 Å

Chemicals

ChemComp-XP4:
1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHATE / DMPA, phospholipid*YM

Source
  • Helicobacter pylori (bacteria)
  • helicobacter pylori (strain j99 / atcc 700824) (bacteria)
KeywordsTRANSPORT PROTEIN / Helicobacter pylori / urea channel / closed state / open state

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