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

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 angstrom 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. Here 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.

Authors:
 [1];  [2];  [3];  [1];  [1];  [1];  [2]
  1. Argonne National Lab. (ANL), Argonne, IL (United States)
  2. Univ. of California, Davis, CA (United States)
  3. Washington State Univ., Richland, WA (United States)
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
National Institutes of Health (NIH); USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)
OSTI Identifier:
1509904
Alternate Identifier(s):
OSTI ID: 1494956
Grant/Contract Number:  
AC02-06CH11357; AC02‐6CH11357
Resource Type:
Accepted Manuscript
Journal Name:
Protein Science
Additional Journal Information:
Journal Volume: 28; Journal Issue: 4; Journal ID: ISSN 0961-8368
Publisher:
The Protein Society
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; CAZyme; Parabacteroides johnsonii; carbohydrate metabolism; cellulase; human gut

Citation Formats

Chang, Changsoo, Brooke, Charles, Piao, Hailan, Mack, Jamey, Babnigg, Gyorgy, Joachimiak, Andrzej, and Hess, Matthias. A 2.08 Å resolution structure of HLB5, a novel cellulase from the anaerobic gut bacterium Parabacteroides johnsonii DSM 18315. United States: N. p., 2019. Web. doi:10.1002/pro.3582.
Chang, Changsoo, Brooke, Charles, Piao, Hailan, Mack, Jamey, Babnigg, Gyorgy, Joachimiak, Andrzej, & Hess, Matthias. A 2.08 Å resolution structure of HLB5, a novel cellulase from the anaerobic gut bacterium Parabacteroides johnsonii DSM 18315. United States. doi:10.1002/pro.3582.
Chang, Changsoo, Brooke, Charles, Piao, Hailan, Mack, Jamey, Babnigg, Gyorgy, Joachimiak, Andrzej, and Hess, Matthias. Sun . "A 2.08 Å resolution structure of HLB5, a novel cellulase from the anaerobic gut bacterium Parabacteroides johnsonii DSM 18315". United States. doi:10.1002/pro.3582.
@article{osti_1509904,
title = {A 2.08 Å resolution structure of HLB5, a novel cellulase from the anaerobic gut bacterium Parabacteroides johnsonii DSM 18315},
author = {Chang, Changsoo and Brooke, Charles and Piao, Hailan and Mack, Jamey and Babnigg, Gyorgy and Joachimiak, Andrzej and Hess, Matthias},
abstractNote = {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 angstrom 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. Here 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.},
doi = {10.1002/pro.3582},
journal = {Protein Science},
number = 4,
volume = 28,
place = {United States},
year = {2019},
month = {1}
}

Journal Article:
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Works referenced in this record:

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