4YZP

Crystal structure of a tri-modular GH5 (subfamily 4) endo-beta-1, 4-glucanase from Bacillus licheniformis

Summary for 4YZP

• Entry DOI: 10.2210/pdb4yzp/pdb
• Descriptor: Cellulose hydrolase (2 entities in total)
• Functional Keywords: endoglucanase, gh5, tri-modular, hydrolase
• Biological source: Bacillus licheniformis
• Total number of polymer chains: 1
• Total formula weight: 60862.36

Authors

Liberato, M.V.,Popov, A.,Polikarpov, I. (deposition date: 2015-03-25, release date: 2016-09-07, Last modification date: 2023-09-27)

Primary citation

Liberato, M.V.,Silveira, R.L.,Prates, E.T.,de Araujo, E.A.,Pellegrini, V.O.,Camilo, C.M.,Kadowaki, M.A.,de O.Neto, M.,Popov, A.,Skaf, M.S.,Polikarpov, I.
Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism.
Sci Rep, 6:23473-23473, 2016

PubMed Abstract: 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.

PubMed: 27032335
DOI: 10.1038/srep23473

Experimental method

X-RAY DIFFRACTION (1.7 Å)