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Title: Natural diversity of glycoside hydrolase family 48 exoglucanases: insights from structure

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 (BpumGH48). 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.

Authors:
 [1];  [1];  [1];  [1];  [2];  [3];  [2];  [1]; ORCiD logo [1];  [1]
  1. National Renewable Energy Lab. (NREL), Golden, CO (United States). Biosciences Center
  2. Cornell Univ., Ithaca, NY (United States). Department of Food Science
  3. Cornell Univ., Ithaca, NY (United States). Biochemistry, Molecular and Cell Biology
Publication Date:
Research Org.:
National Renewable Energy Lab. (NREL), Golden, CO (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)
OSTI Identifier:
1416714
Report Number(s):
NREL/JA-2700-70442
Journal ID: ISSN 1754-6834
Grant/Contract Number:
AC36-08GO28308
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Biotechnology for Biofuels
Additional Journal Information:
Journal Volume: 10; Journal Issue: 1; Journal ID: ISSN 1754-6834
Publisher:
BioMed Central
Country of Publication:
United States
Language:
English
Subject:
09 BIOMASS FUELS; 59 BASIC BIOLOGICAL SCIENCES; GH48; circular dichroism; x-ray crystallography; cellulase; molecular modeling

Citation Formats

Brunecky, Roman, Alahuhta, Markus, Sammond, Deanne W., Xu, Qi, Chen, Mo, Wilson, David B., Brady, John W., Himmel, Michael E., Bomble, Yannick J., and Lunin, Vladimir V.. Natural diversity of glycoside hydrolase family 48 exoglucanases: insights from structure. United States: N. p., 2017. Web. doi:10.1186/s13068-017-0951-5.
Brunecky, Roman, Alahuhta, Markus, Sammond, Deanne W., Xu, Qi, Chen, Mo, Wilson, David B., Brady, John W., Himmel, Michael E., Bomble, Yannick J., & Lunin, Vladimir V.. Natural diversity of glycoside hydrolase family 48 exoglucanases: insights from structure. United States. doi:10.1186/s13068-017-0951-5.
Brunecky, Roman, Alahuhta, Markus, Sammond, Deanne W., Xu, Qi, Chen, Mo, Wilson, David B., Brady, John W., Himmel, Michael E., Bomble, Yannick J., and Lunin, Vladimir V.. Thu . "Natural diversity of glycoside hydrolase family 48 exoglucanases: insights from structure". United States. doi:10.1186/s13068-017-0951-5. https://www.osti.gov/servlets/purl/1416714.
@article{osti_1416714,
title = {Natural diversity of glycoside hydrolase family 48 exoglucanases: insights from structure},
author = {Brunecky, Roman and Alahuhta, Markus and Sammond, Deanne W. and Xu, Qi and Chen, Mo and Wilson, David B. and Brady, John W. and Himmel, Michael E. and Bomble, Yannick J. and Lunin, Vladimir V.},
abstractNote = {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 (BpumGH48). 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.},
doi = {10.1186/s13068-017-0951-5},
journal = {Biotechnology for Biofuels},
number = 1,
volume = 10,
place = {United States},
year = {Thu Nov 30 00:00:00 EST 2017},
month = {Thu Nov 30 00:00:00 EST 2017}
}

Journal Article:
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