| Literature DB >> 30687968 |
Changsoo Chang1,2, Charles Brooke3, Hailan Piao4, Jamey Mack1, Gyorgy Babnigg1, Andrzej Joachimiak1,2, Matthias Hess3.
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 glycosidases. We anticipate that the information presented here will facilitate the identification of additional cellulases for which no homologues have been identified to date and enhance our understanding how these novel cellulases bind and hydrolyze their substrates.Entities:
Keywords: zzm321990Parabacteroides johnsonii; CAZyme; carbohydrate metabolism; cellulase; human gut
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Year: 2019 PMID: 30687968 PMCID: PMC6423722 DOI: 10.1002/pro.3582
Source DB: PubMed Journal: Protein Sci ISSN: 0961-8368 Impact factor: 6.725