Abstract
Cellulases play a significant role in the degradation of complex carbohydrates. In the human gut anaerobic bacteria are essential to the well-being of the host by producing these essential enzymes that convert plant polymers into simple sugars that can then be further metabolized by the host. Here we report the 2.08 Å resolution structure of HLB5, a chemically verified cellulase that was identified previously from an anaerobic gut bacterium and that has no structural cellulase homologues in PDB nor possesses any conserved region typical for enzymes that degrade carbohydrates. We anticipate that the information presented here will facilitate the identification of additional cellulases for which no homologues have been identified until to date and in enhancing our understanding how these novel cellulases bind and hydrolyze their substrates.
Footnotes
Funding: This work was supported by NIH grants GM094585 and GM115586 (to AJ) and the use of Structural Biology Center beamlines was supported by the U.S. Department of Energy, Office of Biological and Environmental Research, under contract DE-AC02—6CH11357.
Conflict of interest: The authors declare no competing interests.