@article{ddd.uab.cat:223394,
      author = {Streltsov, Victor A. and Luang, Sukanya and Peisley, Alys and
               Varghese, Joseph N. and Ketudat Cairns, James R. and Fort,
               Sebastien and Hijnen, Marcel and Tvaroška, Igor and Ardá, Ana
               and Jiménez Barbero, Jesús and Alfonso Prieto, Mercedes and
               Rovira, Carme and Mendoza, Fernanda and Tiessler Sala, Laura. and
               Sánchez-Aparicio, José-Emilio and Rodríguez-Guerra Pedregal,
               Jaime and Lluch López, Josep Maria and Maréchal, Jean-Didier
               and Masgrau, Laura and Hrmova, Maria},
       title = {Discovery of processive catalysis by an exo-hydrolase with a
               pocket-shaped active site},
     journal = {Nature communications},
        year = {2019},
      volume = {10},
       pages = {2222--},
        note = {Altres ajuts: Beatriu de Pinós fellowship BP-B 2013},
    abstract = {Substrates associate and products dissociate from enzyme
               catalytic sites rapidly, which hampers investigations of their
               trajectories. The high-resolution structure of the native Hordeum
               exo-hydrolase HvExoI isolated from seedlings reveals that non-
               covalently trapped glucose forms a stable enzyme-product complex.
               Here, we report that the alkyl β-d-glucoside and methyl
               6-thio-β-gentiobioside substrate analogues perfused in
               crystalline HvExoI bind across the catalytic site after they
               displace glucose, while methyl 2-thio-β-sophoroside attaches
               nearby. Structural analyses and multi-scale molecular modelling
               of nanoscale reactant movements in HvExoI reveal that upon
               productive binding of incoming substrates, the glucose product
               modifies its binding patterns and evokes the formation of a
               transient lateral cavity, which serves as a conduit for glucose
               departure to allow for the next catalytic round. This path
               enables substrate-product assisted processive catalysis through
               multiple hydrolytic events without HvExoI losing contact with
               oligo- or polymeric substrates. We anticipate that such enzyme
               plasticity could be prevalent among exo-hydrolases.},
         doi = {10.1038/s41467-019-09691-z},
         url = {https://ddd.uab.cat/record/223394},
}