Download MendeleyNatural diversity of glycoside hydrolase family 48 exoglucanases: insights from structure.
Brunecky, R., Alahuhta, M., Sammond, D.W., Xu, Q., Chen, M., Wilson, D.B., Brady, J.W., Himmel, M.E., Bomble, Y.J., Lunin, V.V.(2017) Biotechnol Biofuels 10: 274-274
- PubMed: 29213319
- DOI: https://doi.org/10.1186/s13068-017-0951-5
- Primary Citation of Related Structures:
5CVY - PubMed Abstract:
Glycoside hydrolase (GH) family 48 is an understudied and increasingly important exoglucanase family found in the majority of bacterial cellulase systems. Moreover, many thermophilic enzyme systems contain GH48 enzymes. Deletion of GH48 enzymes in these microorganisms results in drastic reduction in biomass deconstruction. Surprisingly, given their importance for these microorganisms, GH48s have intrinsically low cellulolytic activity but even in low ratios synergize greatly with GH9 endoglucanases. In this study, we explore the structural and enzymatic diversity of these enzymes across a wide range of temperature optima. We have crystallized one new GH48 module from Bacillus pumilus in a complex with cellobiose and cellohexaose ( Bpum GH48). We compare this structure to other known GH48 enzymes in an attempt to understand GH48 structure/function relationships and draw general rules correlating amino acid sequences and secondary structures to thermostability in this GH family.
Organizational Affiliation:
Biosciences Center, National Renewable Energy Laboratory, 15013 Denver West Parkway, Golden, CO 80401 USA.
