---
_id: '6859'
abstract:
- lang: eng
  text: V (vacuolar)/A (archaeal)-type adenosine triphosphatases (ATPases), found
    in archaeaand eubacteria, couple ATP hydrolysis or synthesis to proton translocation
    across theplasma membrane using the rotary-catalysis mechanism. They belong to
    the V-typeATPase family, which differs from the mitochondrial/chloroplast F-type
    ATP synthasesin overall architecture. We solved cryo–electron microscopy structures
    of the intactThermus thermophilusV/A-ATPase, reconstituted into lipid nanodiscs,
    in three rotationalstates and two substates. These structures indicate substantial
    flexibility betweenV1and Voin a working enzyme, which results from mechanical
    competition between centralshaft rotation and resistance from the peripheral stalks.
    We also describedetails of adenosine diphosphate inhibition release, V1-Votorque
    transmission, andproton translocation, which are relevant for the entire V-type
    ATPase family.
acknowledged_ssus:
- _id: ScienComp
article_number: eaaw9144
article_processing_charge: No
author:
- first_name: Long
  full_name: Zhou, Long
  id: 3E751364-F248-11E8-B48F-1D18A9856A87
  last_name: Zhou
  orcid: 0000-0002-1864-8951
- first_name: Leonid A
  full_name: Sazanov, Leonid A
  id: 338D39FE-F248-11E8-B48F-1D18A9856A87
  last_name: Sazanov
  orcid: 0000-0002-0977-7989
citation:
  ama: Zhou L, Sazanov LA. Structure and conformational plasticity of the intact Thermus
    thermophilus V/A-type ATPase. <i>Science</i>. 2019;365(6455). doi:<a href="https://doi.org/10.1126/science.aaw9144">10.1126/science.aaw9144</a>
  apa: Zhou, L., &#38; Sazanov, L. A. (2019). Structure and conformational plasticity
    of the intact Thermus thermophilus V/A-type ATPase. <i>Science</i>. AAAS. <a href="https://doi.org/10.1126/science.aaw9144">https://doi.org/10.1126/science.aaw9144</a>
  chicago: Zhou, Long, and Leonid A Sazanov. “Structure and Conformational Plasticity
    of the Intact Thermus Thermophilus V/A-Type ATPase.” <i>Science</i>. AAAS, 2019.
    <a href="https://doi.org/10.1126/science.aaw9144">https://doi.org/10.1126/science.aaw9144</a>.
  ieee: L. Zhou and L. A. Sazanov, “Structure and conformational plasticity of the
    intact Thermus thermophilus V/A-type ATPase,” <i>Science</i>, vol. 365, no. 6455.
    AAAS, 2019.
  ista: Zhou L, Sazanov LA. 2019. Structure and conformational plasticity of the intact
    Thermus thermophilus V/A-type ATPase. Science. 365(6455), eaaw9144.
  mla: Zhou, Long, and Leonid A. Sazanov. “Structure and Conformational Plasticity
    of the Intact Thermus Thermophilus V/A-Type ATPase.” <i>Science</i>, vol. 365,
    no. 6455, eaaw9144, AAAS, 2019, doi:<a href="https://doi.org/10.1126/science.aaw9144">10.1126/science.aaw9144</a>.
  short: L. Zhou, L.A. Sazanov, Science 365 (2019).
date_created: 2019-09-07T19:04:45Z
date_published: 2019-08-23T00:00:00Z
date_updated: 2023-08-29T07:52:02Z
day: '23'
department:
- _id: LeSa
doi: 10.1126/science.aaw9144
external_id:
  isi:
  - '000482464000043'
  pmid:
  - '31439765'
intvolume: '       365'
isi: 1
issue: '6455'
language:
- iso: eng
month: '08'
oa_version: None
pmid: 1
publication: Science
publication_identifier:
  eissn:
  - 1095-9203
  issn:
  - 0036-8075
publication_status: published
publisher: AAAS
quality_controlled: '1'
related_material:
  link:
  - description: News on IST Website
    relation: press_release
    url: https://ist.ac.at/en/news/structure-of-protein-nano-turbine-revealed/
scopus_import: '1'
status: public
title: Structure and conformational plasticity of the intact Thermus thermophilus
  V/A-type ATPase
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 365
year: '2019'
...