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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Effects of the linker region on the structure and function of modular GH5 cellulases

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Author(s):
Ruiz, Diego M. [1] ; Turowski, Valeria R. [1] ; Murakami, Mario T. [1]
Total Authors: 3
Affiliation:
[1] Ctr Nacl Pesquisa Energia & Mat, Lab Nacl Biociencias, BR-13083970 Campinas, SP - Brazil
Total Affiliations: 1
Document type: Journal article
Source: SCIENTIFIC REPORTS; v. 6, JUN 23 2016.
Web of Science Citations: 15
Abstract

The association of glycosyl hydrolases with catalytically inactive modules is a successful evolutionary strategy that is commonly used by biomass-degrading microorganisms to digest plant cell walls. The presence of accessory domains in these enzymes is associated with properties such as higher catalytic efficiency, extension of the catalytic interface and targeting of the enzyme to the proper substrate. However, the importance of the linker region in the synergistic action of the catalytic and accessory domains remains poorly understood. Thus, this study examined how the inter-domain region affects the structure and function of modular GH5 endoglucanases, by using cellulase 5A from Bacillus subtilis (BsCel5A) as a model. BsCel5A variants featuring linkers with different stiffnesses or sizes were designed and extensively characterized, revealing that changes in flexibility or rigidity in this region differentially affect kinetic behavior. Regarding the linker length, we found that precise inter-domain spacing is required to enable efficient hydrolysis because excessively long or short linkers were equally detrimental to catalysis. Together, these findings identify molecular and structural features that may contribute to the rational design of chimeric and multimodular glycosyl hydrolases. (AU)

FAPESP's process: 13/01583-0 - Insights into the molecular basis for specificity and thermal stability in modular bacterial glycoside hydrolases belonging to GH5 family: Bacillus subtilis cellulase and Thermotoga petrophila mannanase.
Grantee:Diego Mario Ruiz
Support type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 13/13309-0 - Studies of the structural and functional behavior of enzymes evolutionarily specialized in the degradation of plant biomass with potential biotechnological applications
Grantee:Mário Tyago Murakami
Support type: Regular Research Grants