Crystal structure of a putative exo-β-1,3-galactanase from Bifidobacterium bifidum S17
Abstract
Given the current interest in second-generation biofuels, carbohydrate-active enzymes have become the most important tool to overcome the structural recalcitrance of the plant cell wall. While some glycoside hydrolase families have been exhaustively described, others remain poorly characterized, especially with regard to structural information. The family 43 glycoside hydrolases are a diverse group of inverting enzymes; the available structure information on these enzymes is mainly from xylosidases and arabinofuranosidase. Currently, only one structure of an exo-β-1,3-galactanase is available. Here, the production, crystallization and structure determination of a putative exo-β-1,3-galactanase fromBifidobacterium bifidumS17 (BbGal43A) are described.BbGal43A was successfully produced and showed activity towards synthetic galactosides.BbGal43A was subsequently crystallized and data were collected to 1.4 Å resolution. The structure shows a single-domain molecule, differing from known homologues, and crystal contact analysis predicts the formation of a dimer in solution. Further biochemical studies are necessary to elucidate the differences betweenBbGal43A and its characterized homologues.
- Authors:
- Publication Date:
- Research Org.:
- Brookhaven National Lab. (BNL), Upton, NY (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- OSTI Identifier:
- 1354311
- Report Number(s):
- BNL-112827-2016-JA
Journal ID: ISSN 2053-230X; ACSFEN
- DOE Contract Number:
- SC00112704
- Resource Type:
- Journal Article
- Journal Name:
- Acta Crystallographica. Section F, Structural Biology Communications
- Additional Journal Information:
- Journal Volume: 72; Journal Issue: 4; Journal ID: ISSN 2053-230X
- Publisher:
- International Union of Crystallography
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; galactanase; Bifidobacterium; GH43; family 43; hydrolase.
Citation Formats
Godoy, Andre S., de Lima, Mariana Z. T., Camilo, Cesar M., and Polikarpov, Igor. Crystal structure of a putative exo-β-1,3-galactanase from Bifidobacterium bifidum S17. United States: N. p., 2016.
Web. doi:10.1107/S2053230X16003617.
Godoy, Andre S., de Lima, Mariana Z. T., Camilo, Cesar M., & Polikarpov, Igor. Crystal structure of a putative exo-β-1,3-galactanase from Bifidobacterium bifidum S17. United States. https://doi.org/10.1107/S2053230X16003617
Godoy, Andre S., de Lima, Mariana Z. T., Camilo, Cesar M., and Polikarpov, Igor. 2016.
"Crystal structure of a putative exo-β-1,3-galactanase from Bifidobacterium bifidum S17". United States. https://doi.org/10.1107/S2053230X16003617.
@article{osti_1354311,
title = {Crystal structure of a putative exo-β-1,3-galactanase from Bifidobacterium bifidum S17},
author = {Godoy, Andre S. and de Lima, Mariana Z. T. and Camilo, Cesar M. and Polikarpov, Igor},
abstractNote = {Given the current interest in second-generation biofuels, carbohydrate-active enzymes have become the most important tool to overcome the structural recalcitrance of the plant cell wall. While some glycoside hydrolase families have been exhaustively described, others remain poorly characterized, especially with regard to structural information. The family 43 glycoside hydrolases are a diverse group of inverting enzymes; the available structure information on these enzymes is mainly from xylosidases and arabinofuranosidase. Currently, only one structure of an exo-β-1,3-galactanase is available. Here, the production, crystallization and structure determination of a putative exo-β-1,3-galactanase fromBifidobacterium bifidumS17 (BbGal43A) are described.BbGal43A was successfully produced and showed activity towards synthetic galactosides.BbGal43A was subsequently crystallized and data were collected to 1.4 Å resolution. The structure shows a single-domain molecule, differing from known homologues, and crystal contact analysis predicts the formation of a dimer in solution. Further biochemical studies are necessary to elucidate the differences betweenBbGal43A and its characterized homologues.},
doi = {10.1107/S2053230X16003617},
url = {https://www.osti.gov/biblio/1354311},
journal = {Acta Crystallographica. Section F, Structural Biology Communications},
issn = {2053-230X},
number = 4,
volume = 72,
place = {United States},
year = {Wed Mar 16 00:00:00 EDT 2016},
month = {Wed Mar 16 00:00:00 EDT 2016}
}