Crystal Structure of Glycoside Hydrolase Family 127 ..beta..-L-arabinofuranosidase from Bifidobacterium longum

Ito, T.; Saikawa, K.; Kim, S.; Fujita, K.; Ishiwata, A.; Kaeothip, S.; Arakawa, T.; Wakagi, T.; Beckham, G. T.; Ito, Y.; Fushinobu, S.

doi:10.1016/j.bbrc.2014.03.096

Title: Crystal Structure of Glycoside Hydrolase Family 127 ..beta..-L-arabinofuranosidase from Bifidobacterium longum

Full Record
Other Related Research

Authors:: Ito, T.; Saikawa, K.; Kim, S.; Fujita, K.; Ishiwata, A.; Kaeothip, S.; Arakawa, T.; Wakagi, T.; Beckham, G. T.; Ito, Y.; Fushinobu, S.

Publication Date:: Fri Apr 25 00:00:00 EDT 2014

Research Org.:: National Renewable Energy Lab. (NREL), Golden, CO (United States)

Sponsoring Org.:: Japan Society for the Promotion of Science (JSPS); USDOE BioEnergy Technologies Office; NREL Laboratory Directed Research and Development (LDRD) Program

OSTI Identifier:: 1134139

DOE Contract Number:: AC36-08GO28308

Resource Type:: Journal Article

Journal Name:: Biochemical and Biophysical Research Communications

Additional Journal Information:: Journal Volume: 447; Journal Issue: 1, 25 April 2014

Country of Publication:: United States

Language:: English

Subject:: 59 BASIC BIOLOGICAL SCIENCES; 37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; Bioenergy

Citation Formats


                    Ito, T., Saikawa, K., Kim, S., Fujita, K., Ishiwata, A., Kaeothip, S., Arakawa, T., Wakagi, T., Beckham, G. T., Ito, Y., and Fushinobu, S. Crystal Structure of Glycoside Hydrolase Family 127 ..beta..-L-arabinofuranosidase from Bifidobacterium longum.  United States: N. p., 2014. 
        Web.  doi:10.1016/j.bbrc.2014.03.096.

Copy to clipboard


                    Ito, T., Saikawa, K., Kim, S., Fujita, K., Ishiwata, A., Kaeothip, S., Arakawa, T., Wakagi, T., Beckham, G. T., Ito, Y., & Fushinobu, S. Crystal Structure of Glycoside Hydrolase Family 127 ..beta..-L-arabinofuranosidase from Bifidobacterium longum.  United States.  https://doi.org/10.1016/j.bbrc.2014.03.096

Copy to clipboard


                    Ito, T., Saikawa, K., Kim, S., Fujita, K., Ishiwata, A., Kaeothip, S., Arakawa, T., Wakagi, T., Beckham, G. T., Ito, Y., and Fushinobu, S. 2014.  
        "Crystal Structure of Glycoside Hydrolase Family 127 ..beta..-L-arabinofuranosidase from Bifidobacterium longum".  United States.  https://doi.org/10.1016/j.bbrc.2014.03.096.

Copy to clipboard


                    
@article{osti_1134139,

  title        = {Crystal Structure of Glycoside Hydrolase Family 127 ..beta..-L-arabinofuranosidase from Bifidobacterium longum},

  author       = {Ito, T. and Saikawa, K. and Kim, S. and Fujita, K. and Ishiwata, A. and Kaeothip, S. and Arakawa, T. and Wakagi, T. and Beckham, G. T. and Ito, Y. and Fushinobu, S.},

  abstractNote = {},

  doi          = {10.1016/j.bbrc.2014.03.096},

  url          = {https://www.osti.gov/biblio/1134139},
  journal      = {Biochemical and Biophysical Research Communications},
number       = 1, 25 April 2014,

  volume       = 447,

  place        = {United States},

  year         = {Fri Apr 25 00:00:00 EDT 2014},

  month        = {Fri Apr 25 00:00:00 EDT 2014}

}

Copy to clipboard

Journal Article:

https://doi.org/10.1016/j.bbrc.2014.03.096

Other availability

Find in Google Scholar

Search WorldCat to find libraries that may hold this journal

Save / Share:

Export Metadata

Save to My Library

Similar records in OSTI.GOV collections:

Crystal structure of glycoside hydrolase family 127 β-L-arabinofuranosidase from Bifidobacterium longum

Journal Article Ito, Tasuku; Saikawa, Kyo; Kim, Seonah; ... - Biochemical and Biophysical Research Communications

Graphical abstract: - Highlights: • HypBA1 β-L-arabinofuranosidase belongs to glycoside hydrolase family 127. • Crystal structure of HypBA1 was determined. • HypBA1 consists of a catalytic barrel and two additional β-sandwich domains. • The active site contains a Zn{sup 2+} coordinated by glutamate and three cysteines. • A possible reaction mechanism involving cysteine as the nucleophile is proposed. - Abstract: Enzymes acting on β-linked arabinofuranosides have been unknown until recently, in spite of wide distribution of β-L-arabinofuranosyl oligosaccharides in plant cells. Recently, a β-L-arabinofuranosidase from the glycoside hydrolase family 127 (HypBA1) was discovered in the newly characterized degradation system ofmore »« less
https://doi.org/10.1016/J.BBRC.2014.03.096
Loop Motions Important to Product Expulsion in the Thermobifida fusca Glycoside Hydrolase Family 6 Cellobiohydrolase from Structural and Computational Studies

Journal Article Wu, M.; Bu, L.; Vuong, T.; ... - Journal of Biological Chemistry
https://doi.org/10.1074/jbc.M113.502765
Natural diversity of glycoside hydrolase family 48 exoglucanases: insights from structure

Journal Article Brunecky, Roman; Alahuhta, Markus; Sammond, Deanne; ... - Biotechnology for Biofuels

Glycoside hydrolase (GH) family 48 is an understudied and increasingly important exoglucanase family found in the majority of bacterial cellulase systems. Moreover, many thermophilic enzyme systems contain GH48 enzymes. Deletion of GH48 enzymes in these microorganisms results in drastic reduction in biomass deconstruction. Surprisingly, given their importance for these microorganisms, GH48s have intrinsically low cellulolytic activity but even in low ratios synergize greatly with GH9 endoglucanases. In this study, we explore the structural and enzymatic diversity of these enzymes across a wide range of temperature optima. We have crystallized one new GH48 module from Bacillus pumilus in a complex withmore »« less
Cited by 9
https://doi.org/10.1186/s13068-017-0951-5
The Structure and Function of an Arabinan-specific [alpha]-1,2-Arabinofuranosidase Identified from Screening the Activities of Bacterial GH43 Glycoside Hydrolases

Journal Article Cartmell, Alan; McKee, Lauren; Pena, Maria; ... - Journal of Biological Chemistry

Reflecting the diverse chemistry of plant cell walls, microorganisms that degrade these composite structures synthesize an array of glycoside hydrolases. These enzymes are organized into sequence-, mechanism-, and structure-based families. Genomic data have shown that several organisms that degrade the plant cell wall contain a large number of genes encoding family 43 (GH43) glycoside hydrolases. Here we report the biochemical properties of the GH43 enzymes of a saprophytic soil bacterium, Cellvibrio japonicus, and a human colonic symbiont, Bacteroides thetaiotaomicron. The data show that C. japonicus uses predominantly exo-acting enzymes to degrade arabinan into arabinose, whereas B. thetaiotaomicron deploys a combinationmore »« less
https://doi.org/10.1074/jbc.M110.215962
Crystal structure of a type II dehydroquinate dehydratase-like protein from Bifidobacterium longum

Journal Article Light, Samuel; Krishna, Sankar; Bergan, Raymond; ... - Journal of Structural and Functional Genomics
https://doi.org/10.1007/s10969-013-9149-7

Similar Records