Motor protein structure articles within Nature Communications

Featured

• Article
  27 July 2023 | Open Access

  Ion selectivity and rotor coupling of the Vibrio flagellar sodium-driven stator unit

  In this work, the authors provide mechanistic insights for understanding the sodium-dependent, bacterial flagellar stator unit PomAB ion selectivity, directional rotation, and rotor incorporation in Vibrio spp.

  • Haidai Hu
  • , Philipp F. Popp
  •  & Nicholas M. I. Taylor

• Article
  22 July 2021 | Open Access

  Structure of the molecular bushing of the bacterial flagellar motor

  In the basal body of the bacterial flagellum, the LP ring acts as a bushing supporting the distal rod for its rapid and stable rotation. Here, Yamaguchi et al. present the electron cryomicroscopy structure of the LP ring around the rod, shedding light into potential mechanisms involved in stability and assembly of the structure.

  • Tomoko Yamaguchi
  • , Fumiaki Makino
  •  & Keiichi Namba

• Article
  10 November 2020 | Open Access

  A tunable LIC1-adaptor interaction modulates dynein activity in a cargo-specific manner

  Activating adaptors that link dynein to its general cofactor dynactin recruit specific cargoes and regulate dynein’s activity and processive motility in retrograde transport. Here, the authors present the crystal structures of two adaptor complexes with the dynein light intermediate chain-1 (LIC1) and show that activating adaptors can be grouped into three structural classes based on their different interactions with LIC1.

  • In-Gyun Lee
  • , Sydney E. Cason
  •  & Roberto Dominguez

• Article
  25 February 2020 | Open Access

  Structural basis for two-way communication between dynein and microtubules

  The movement of cytoplasmic dynein on microtubule tracks is coordinated by the microtubule-binding domain (MTBD) and the ATPase domain via a coiled-coil stalk. Here authors use NMR and cryo-EM and suggest that the communication between the ATPase-domain and MTBD is achieved by sliding of the stalk α-helix by a half-turn or one-turn.

  • Noritaka Nishida
  • , Yuta Komori
  •  & Masahide Kikkawa

• Article
  25 April 2018 | Open Access

  Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s

  Kinesin-13s are microtubule depolymerases that lack motile activity. Here the authors present the cryo-EM structures of kinesin-13 microtubule complexes in different nucleotide bound states, which reveal how ATP hydrolysis is linked to conformational changes and propose a model for kinesin induced depolymerisation.

  • Matthieu P.M.H. Benoit
  • , Ana B. Asenjo
  •  & Hernando Sosa

• Article
  09 January 2017 | Open Access

  Structure of actomyosin rigour complex at 5.2 Å resolution and insights into the ATPase cycle mechanism

  The cyclic association and dissociation of myosin with actin filament is regulated by ATP binding and hydrolysis cycles. Here the authors report the structure of mammalian skeletal muscle actomyosin rigour complex that provides insights into the ATPase-coupled reaction cycle of actomyosin.

  • Takashi Fujii
  •  & Keiichi Namba

• Article
  01 September 2016 | Open Access

  The myosin X motor is optimized for movement on actin bundles

  Myosin X is a molecular motor unique in its ability to generate filopodia, but the mechanism explaining this behaviour is not known. Here, through a combination of structure, single-molecule assays and modelling the authors show that myosin X is optimized for transport along actin bundles.

  • Virginie Ropars
  • , Zhaohui Yang
  •  & Anne Houdusse

• Article
  14 September 2015 | Open Access

  Direct observation shows superposition and large scale flexibility within cytoplasmic dynein motors moving along microtubules

  Cytoplasmic dynein is a dimeric protein that steps processively along microtubules. Here Imaiet al. present cryo-electron microscopy images of stepping D. discoideumdynein, revealing diverse microtubule-bound configurations including a hinge-dependent, motors side-by-side arrangement.

  • Hiroshi Imai
  • , Tomohiro Shima
  •  & Stan A. Burgess

• Article | 14 November 2014

  The structure of apo-kinesin bound to tubulin links the nucleotide cycle to movement

  A complete description of how the motor protein kinesin-1 walks along microtubules is missing because of the lack of a key structure. Here, Cao et al. solve the apo-kinesin:microtubule structure, completing the structure set and permitting the description of the structural changes that occur during the nucleotide cycle and their functional consequences.

  • Luyan Cao
  • , Weiyi Wang
  •  & Benoît Gigant