Selected article for: "active form and loop interface"
Author: Megan C. Cohan; Ammon E. Posey; Steven J. Grigsby; Anuradha Mittal; Alex S. Holehouse; Paul J. Buske; Petra A. Levin; Rohit V. Pappu
Title: Evolved sequence features within the intrinsically disordered tail influence FtsZ assembly and bacterial cell division
  • Document date: 2018_4_14
    • ID: 2rzfuy33_35
    Snippet: In vitro polymerization, bundling, and GTPase activity of CTLV4 is comparable to that of WT: The GTP binding site and the T7 activation loop that is required for the catalytic activity are on opposite sides of the core domain of FtsZ. Accordingly, the active form of the enzyme is a dimer and GTP is hydrolyzed at the interface of the GTP binding site and the T7 loop ( Figure S4A ). GTP binding promotes dimerization and the formation of higher-orde.....
    Document: In vitro polymerization, bundling, and GTPase activity of CTLV4 is comparable to that of WT: The GTP binding site and the T7 activation loop that is required for the catalytic activity are on opposite sides of the core domain of FtsZ. Accordingly, the active form of the enzyme is a dimer and GTP is hydrolyzed at the interface of the GTP binding site and the T7 loop ( Figure S4A ). GTP binding promotes dimerization and the formation of higher-order headto-tail polymers of FtsZ. In the dimeric state, GTP hydrolysis at the subunit interface leads to dissociation into two monomers (Scheffers et al., 2002) . In the polymeric form, GTP hydrolysis promotes bending and ring formation (Erickson et al., 2010) .

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