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TitleMolecular architecture of the N-type ATPase rotor ring from .
Journal, issue, pagesEMBO Rep, Vol. 18, Issue 4, Page 526-535, Year 2017
Publish dateMar 10, 2017
AuthorsSarah Schulz / Martin Wilkes / Deryck J Mills / Werner Kühlbrandt / Thomas Meier /
PubMed AbstractThe genome of the highly infectious bacterium harbors an operon that encodes an N-type rotary ATPase, in addition to an operon for a regular F-type rotary ATPase. The molecular architecture of N- ...The genome of the highly infectious bacterium harbors an operon that encodes an N-type rotary ATPase, in addition to an operon for a regular F-type rotary ATPase. The molecular architecture of N-type ATPases is unknown and their biochemical properties and cellular functions are largely unexplored. We studied the NN-type ATPase and investigated the structure and ion specificity of its membrane-embedded c-ring rotor by single-particle electron cryo-microscopy. Of several amphiphilic compounds tested for solubilizing the complex, the choice of the low-density, low-CMC detergent LDAO was optimal in terms of map quality and resolution. The cryoEM map of the c-ring at 6.1 Å resolution reveals a heptadecameric oligomer with a molecular mass of ~141 kDa. Biochemical measurements indicate that the c ring is H specific, demonstrating that the ATPase is proton-coupled. The c ring stoichiometry results in a very high ion-to-ATP ratio of 5.7. We propose that this N-ATPase is a highly efficient proton pump that helps these melioidosis-causing bacteria to survive in the hostile, acidic environment of phagosomes.
External linksEMBO Rep / PubMed:28283532 / PubMed Central
MethodsEM (single particle)
Resolution6.1 Å
Structure data

EMDB-3546:
Structure of a novel N-type ATPase rotor ring (c17) from Burkholderia pseudomallei
Method: EM (single particle) / Resolution: 6.1 Å

Source
  • Burkholderia pseudomallei (bacteria)

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