Literature DB >> 30687968

A 2.08 Å resolution structure of HLB5, a novel cellulase from the anaerobic gut bacterium Parabacteroides johnsonii DSM 18315.

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.
© 2019 The Protein Society.

Entities:  

Keywords:  zzm321990Parabacteroides johnsonii; CAZyme; carbohydrate metabolism; cellulase; human gut

Mesh:

Substances:

Year:  2019        PMID: 30687968      PMCID: PMC6423722          DOI: 10.1002/pro.3582

Source DB:  PubMed          Journal:  Protein Sci        ISSN: 0961-8368            Impact factor:   6.725


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