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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 Laboratory (ANL), Argonne, IL (United States)
Sponsoring Org.:
National Institutes of Health (NIH); USDOE Office of Science (SC), Biological and Environmental Research (BER)
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. https://doi.org/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. https://doi.org/10.1002/pro.3582. https://www.osti.gov/servlets/purl/1509904.
@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 = {Sun Jan 27 00:00:00 EST 2019},
month = {Sun Jan 27 00:00:00 EST 2019}
}

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Works referenced in this record:

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids
journal, May 2007

  • Davis, I. W.; Leaver-Fay, A.; Chen, V. B.
  • Nucleic Acids Research, Vol. 35, Issue Web Server
  • DOI: 10.1093/nar/gkm216

A New Vector for High-Throughput, Ligation-Independent Cloning Encoding a Tobacco Etch Virus Protease Cleavage Site
journal, June 2002

  • Stols, Lucy; Gu, Minyi; Dieckman, Lynda
  • Protein Expression and Purification, Vol. 25, Issue 1
  • DOI: 10.1006/prep.2001.1603

Microbial Cellulose Utilization: Fundamentals and Biotechnology
journal, September 2002

  • Lynd, L. R.; Weimer, P. J.; van Zyl, W. H.
  • Microbiology and Molecular Biology Reviews, Vol. 66, Issue 3, p. 506-577
  • DOI: 10.1128/MMBR.66.3.506-577.2002

Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
journal, June 2008

  • Langer, Gerrit; Cohen, Serge X.; Lamzin, Victor S.
  • Nature Protocols, Vol. 3, Issue 7
  • DOI: 10.1038/nprot.2008.91

Dali server update
journal, April 2016

  • Holm, Liisa; Laakso, Laura M.
  • Nucleic Acids Research, Vol. 44, Issue W1
  • DOI: 10.1093/nar/gkw357

HKL -3000: the integration of data reduction and structure solution – from diffraction images to an initial model in minutes
journal, July 2006

  • Minor, Wladek; Cymborowski, Marcin; Otwinowski, Zbyszek
  • Acta Crystallographica Section D Biological Crystallography, Vol. 62, Issue 8
  • DOI: 10.1107/S0907444906019949

Coot model-building tools for molecular graphics
journal, November 2004

  • Emsley, Paul; Cowtan, Kevin
  • Acta Crystallographica Section D Biological Crystallography, Vol. 60, Issue 12, p. 2126-2132
  • DOI: 10.1107/S0907444904019158

The carbohydrate-active enzymes database (CAZy) in 2013
journal, November 2013

  • Lombard, Vincent; Golaconda Ramulu, Hemalatha; Drula, Elodie
  • Nucleic Acids Research, Vol. 42, Issue D1
  • DOI: 10.1093/nar/gkt1178

Inference of Macromolecular Assemblies from Crystalline State
journal, September 2007


Microbial Cellulases and Their Industrial Applications
journal, January 2011

  • Kuhad, Ramesh Chander; Gupta, Rishi; Singh, Ajay
  • Enzyme Research, Vol. 2011
  • DOI: 10.4061/2011/280696

Cellulosic ethanol: status and innovation
journal, June 2017


PHENIX: a comprehensive Python-based system for macromolecular structure solution
journal, January 2010

  • Adams, Paul D.; Afonine, Pavel V.; Bunkóczi, Gábor
  • Acta Crystallographica Section D Biological Crystallography, Vol. 66, Issue 2, p. 213-221
  • DOI: 10.1107/S0907444909052925

Synthesis, regulation and utilization of lignocellulosic biomass
journal, April 2010


An insight into nanocellulose as soft condensed matter: Challenge and future prospective toward environmental sustainability
journal, February 2019