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

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.

doi:10.1186/s13068-017-0951-5

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

Journal Article · Thu Nov 30 00:00:00 EST 2017 · Biotechnology for Biofuels

DOI:https://doi.org/10.1186/s13068-017-0951-5· OSTI ID:1618693

Brunecky, Roman; Alahuhta, Markus; Sammond, Deanne W.; Xu, Qi; Chen, Mo; Wilson, David B.; Brady, John W.; Himmel, Michael E.;

; Lunin, Vladimir V.

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.

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Research Organization:: National Renewable Energy Laboratory (NREL), Golden, CO (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER)

Grant/Contract Number:: AC36-08GO28308

OSTI ID:: 1618693

Alternate ID(s):: OSTI ID: 1416714

Report Number(s):: NREL/JA-2700-70442; 274; PII: 951

Journal Information:: Biotechnology for Biofuels, Journal Name: Biotechnology for Biofuels Vol. 10 Journal Issue: 1; ISSN 1754-6834

Publisher:: Springer Science + Business MediaCopyright Statement

Country of Publication:: Netherlands

Language:: English

Citation Metrics:

Cited by: 9 works

Citation information provided by
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Aromatic residues surrounding the active site tunnel of TfCel48A influence activity, processivity, and synergistic interactions with other cellulases Hefferon, Kathleen L.; Cantero‐Tubilla, Borja; Brady, John Biotechnology and Bioengineering, Vol. 116, Issue 10 https://doi.org/10.1002/bit.27086	journal	July 2019
Metabolic engineering of Clostridium thermocellum for n-butanol production from cellulose Tian, Liang; Conway, Peter M.; Cervenka, Nicholas D. Biotechnology for Biofuels, Vol. 12, Issue 1 https://doi.org/10.1186/s13068-019-1524-6	journal	July 2019
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09 BIOMASS FUELS
59 BASIC BIOLOGICAL SCIENCES
GH48
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MOESM1 of Natural diversity of glycoside hydrolase family 48 exoglucanases: insights from structure Brunecky, Roman; Alahuhta, Markus; Sammond, Deanne https://doi.org/10.6084/m9.figshare.5649085.v1 The current record is supplemented by this dataset	dataset	November 2017
Natural diversity of glycoside hydrolase family 48 exoglucanases: insights from structure Brunecky, Roman; Alahuhta, Markus; Sammond, Deanne https://doi.org/10.6084/m9.figshare.c.3942418 The current record is supplemented by this dataset	dataset	November 2017
Natural diversity of glycoside hydrolase family 48 exoglucanases: insights from structure Brunecky, Roman; Alahuhta, Markus; Sammond, Deanne https://doi.org/10.6084/m9.figshare.c.3942418.v1 The current record is supplemented by this collection	collection	November 2017