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Showing 1–4 of 4 results
Advanced filters: Author: Byung-Gil Lee Clear advanced filters
  • Cryo-EM structures of the S. cerevisiae condensin holo complex reveal that ATP binding triggers exchange of the two HEAT-repeat subunits bound to the SMC ATPase head domains, potentially leading to an interconversion of DNA-binding sites in the catalytic core of condensin that might form the basis of its DNA translocation and loop-extrusion activities.

    • Byung-Gil Lee
    • Fabian Merkel
    • Christian H. Haering
    Research
    Nature Structural & Molecular Biology
    Volume: 27, P: 743-751
  • The bacterial protease ClpP forms an active complex with Clp-ATPases, but can also be directly activated by a recently characterized class of antibiotics (ADEP). Now the crystal structures of Bacillus subtilis ClpP bound to ADEPs reveal the conformational changes involved in ClpP's activation.

    • Byung-Gil Lee
    • Eun Young Park
    • Hyun Kyu Song
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 471-478
  • Two evolutionarily distant SMC–kleisin complexes are shown to contain a bendable coiled-coil discontinuity near the middle of their arms, which permits a folded conformation with potential implications for DNA loading and translocation.

    • Frank Bürmann
    • Byung-Gil Lee
    • Jan Löwe
    Research
    Nature Structural & Molecular Biology
    Volume: 26, P: 227-236