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

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

doi:10.1107/s0907444912001680

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

Journal Article · Thu Mar 01 04:00:00 EST 2012 · Acta Crystallographica Section D: Biological Crystallography

DOI:https://doi.org/10.1107/s0907444912001680· OSTI ID:1045735

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

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.

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

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23), National Science Foundation (NSF)

DOE Contract Number:: AC36-08GO28308

OSTI ID:: 1045735

Report Number(s):: NREL/JA-2700-54450

Journal Information:: Acta Crystallographica Section D: Biological Crystallography, Journal Name: Acta Crystallographica Section D: Biological Crystallography Journal Issue: 3 Vol. 68

Country of Publication:: United States

Language:: English

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