Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/320529
Type: Artigo de Periódico
Title: Molecular Characterization Of A Family 5 Glycoside Hydrolase Suggests An Induced-fit Enzymatic Mechanism
Author: Liberato
MV; Silveira
RL; Prates
ET; de Araujo
EA; Pellegrini
VOA; Camilo
CM; Kadowaki
MA; Neto
MD; Popov
A; Skaf
MS; Polikarpov
I
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.
Subject: Carbohydrate-binding Modules
Biological Macromolecules
Conformational Selection
Structural-characterization
Solution Scattering
Crystal-structure
Dynamics
Recognition
Proteins
Server
Editor: NATURE PUBLISHING GROUP
Citation: Scientific Reports. NATURE PUBLISHING GROUP, n. 6, n. 23473, p. .
Rights: aberto
Identifier DOI: 10.1038/srep23473
Address: http://www-nature-com.ez88.periodicos.capes.gov.br/articles/srep23473
Date Issue: 2016
Appears in Collections:Unicamp - Artigos e Outros Documentos

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