Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism
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2016-04-01
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Liberato, Marcelo V.
Silveira, Rodrigo L.
Prates, Erica T.
Araujo, Evandro A. de
Pellegrini, Vanessa O. A.
Camilo, Cesar M.
Kadowaki, Marco A.
Neto, Mario de O. [UNESP]
Popov, Alexander
Skaf, Munir S.
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Nature Publishing Group
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Glycoside hydrolases (GHs) play fundamental roles in the decomposition of lignocellulosic biomaterials. Here, we report the full-length structure of a cellulase from Bacillus licheniformis (BlCel5B), a member of the GH5 subfamily 4 that is entirely dependent on its two ancillary modules (Ig-like module and CBM46) for catalytic activity. Using X-ray crystallography, small-angle X-ray scattering and molecular dynamics simulations, we propose that the C-terminal CBM46 caps the distal N-terminal catalytic domain (CD) to establish a fully functional active site via a combination of large-scale multidomain conformational selection and induced-fit mechanisms. The Ig-like module is pivoting the packing and unpacking motions of CBM46 relative to CD in the assembly of the binding subsite. This is the first example of a multidomain GH relying on large amplitude motions of the CBM46 for assembly of the catalytically competent form of the enzyme.
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Scientific Reports. London: Nature Publishing Group, v. 6, 15 p., 2016.