Structure and Function of the Clostridium thermocellum Cellobiohydrolase A X1-Module Repeat: Enhancement Through Stabilization of the CbhA Complex

Roman Brunecky, Markus Alahuhta, Yannick J. Bomble, Qi Xu, John O. Baker, Shi You Ding, Michael E. Himmel, Vladimir V. Lunin

Research output: Contribution to journalArticlepeer-review

14 Scopus Citations

Abstract

The efficient deconstruction of lignocellulosic biomass remains a significant barrier to the commercialization of biofuels. Whereas most commercial plant cell-wall-degrading enzyme preparations used today are derived from fungi, the cellulosomal enzyme system from Clostridium thermocellum is an equally effective catalyst, yet of considerably different structure. A key difference between fungal enzyme systems and cellulosomal enzyme systems is that cellulosomal enzyme systems utilize self-assembled scaffolded multimodule enzymes to deconstruct biomass. Here, the possible function of the X1 modules in the complex multimodular enzyme system cellobiohydrolase A (CbhA) from C. thermocellum is explored. The crystal structures of the two X1 modules from C. thermocellum CbhA have been solved individually and together as one construct. The role that calcium may play in the stability of the X1 modules has also been investigated, as well as the possibility that they interact with each other. Furthermore, the results show that whereas the X1 modules do not seem to act as cellulose disruptors, they do aid in the thermostability of the CbhA complex, effectively allowing it to deconstruct cellulose at a higher temperature.

Original languageAmerican English
Pages (from-to)292-299
Number of pages8
JournalActa Crystallographica Section D: Biological Crystallography
Volume68
Issue number3
DOIs
StatePublished - Mar 2012

NREL Publication Number

  • NREL/JA-2700-54450

Keywords

  • CbhA
  • cellulose degradation
  • cellulosome
  • fibronectin III
  • X1 modules

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