Natural Diversity of Glycoside Hydrolase Family 48 Exoglucanases: Insights from Structure

Yannick Bomble, Roman Brunecky, Petri Alahuhta, Qi Xu, Michael Himmel, Vladimir Lunin, Mo Chen, David Wilson, John Brady, Deanne Sammond

Research output: Contribution to journalArticlepeer-review

10 Scopus Citations

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.

Original languageAmerican English
Article number274
Number of pages9
JournalBiotechnology for Biofuels
Volume10
Issue number1
DOIs
StatePublished - 2017

Bibliographical note

Publisher Copyright:
© 2017 The Author(s).

NREL Publication Number

  • NREL/JA-2700-70442

Keywords

  • Cellulase
  • Circular dichroism
  • GH48
  • Molecular modeling
  • X-ray crystallography

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