Publication

Crystal Structure of 4,6-α-Glucanotransferase Supports Diet-Driven Evolution of GH70 Enzymes from α-Amylases in Oral Bacteria

Bai, Y., Gangoiti, J., Dijkstra, B. W., Dijkhuizen, L. & Pijning, T., 7-Feb-2017, In : Structure. 25, 2, p. 231-242 12 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Bai, Y., Gangoiti , J., Dijkstra, B. W., Dijkhuizen, L., & Pijning, T. (2017). Crystal Structure of 4,6-α-Glucanotransferase Supports Diet-Driven Evolution of GH70 Enzymes from α-Amylases in Oral Bacteria. Structure, 25(2), 231-242. https://doi.org/10.1016/j.str.2016.11.023

Author

Bai, Yuxiang ; Gangoiti , Joana ; Dijkstra, Bauke W ; Dijkhuizen, Lubbert ; Pijning, Tjaard. / Crystal Structure of 4,6-α-Glucanotransferase Supports Diet-Driven Evolution of GH70 Enzymes from α-Amylases in Oral Bacteria. In: Structure. 2017 ; Vol. 25, No. 2. pp. 231-242.

Harvard

Bai, Y, Gangoiti , J, Dijkstra, BW, Dijkhuizen, L & Pijning, T 2017, 'Crystal Structure of 4,6-α-Glucanotransferase Supports Diet-Driven Evolution of GH70 Enzymes from α-Amylases in Oral Bacteria', Structure, vol. 25, no. 2, pp. 231-242. https://doi.org/10.1016/j.str.2016.11.023

Standard

Crystal Structure of 4,6-α-Glucanotransferase Supports Diet-Driven Evolution of GH70 Enzymes from α-Amylases in Oral Bacteria. / Bai, Yuxiang; Gangoiti , Joana; Dijkstra, Bauke W; Dijkhuizen, Lubbert; Pijning, Tjaard.

In: Structure, Vol. 25, No. 2, 07.02.2017, p. 231-242.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Bai Y, Gangoiti J, Dijkstra BW, Dijkhuizen L, Pijning T. Crystal Structure of 4,6-α-Glucanotransferase Supports Diet-Driven Evolution of GH70 Enzymes from α-Amylases in Oral Bacteria. Structure. 2017 Feb 7;25(2):231-242. https://doi.org/10.1016/j.str.2016.11.023


BibTeX

@article{bda87c2ad3bb48e9b0a4586730fc9634,
title = "Crystal Structure of 4,6-α-Glucanotransferase Supports Diet-Driven Evolution of GH70 Enzymes from α-Amylases in Oral Bacteria",
abstract = "Food processing and refining has dramatically changed the human diet, but little is known about whether this affected the evolution of enzymes in human microbiota. We present evidence that glycoside hydrolase family 70 (GH70) glucansucrases from lactobacilli, synthesizing α-glucan-type extracellular polysaccharides from sucrose, likely evolved from GH13 starch-acting α-amylases, via GH70 4,6-α-glucanotransferases. The crystal structure of a 4,6-α-glucanotransferase explains the mode of action and unique product specificity of these enzymes. While the α-amylase substrate-binding scaffold is retained, active-site loops adapted to favor transglycosylation over hydrolysis; the structure also gives clues as to how 4,6-α-glucanotransferases may have evolved further toward sucrose utilization instead of starch. Further supported by genomic, phylogenetic, and in vivo studies, we propose that dietary changes involving starch (and starch derivatives) and sucrose intake were critical factors during the evolution of 4,6-α-GTs and glucansucrases from α-amylases, allowing oral bacteria to produce extracellular polymers that contribute to biofilm formation from different substrates.",
keywords = "4,6-α-Glucanotransferase, Crystal structure, Starch, Lactobacillus reuteri, Dental caries, Lactic Acid Bacteria",
author = "Yuxiang Bai and Joana Gangoiti and Dijkstra, {Bauke W} and Lubbert Dijkhuizen and Tjaard Pijning",
note = "Copyright {\textcopyright} 2016 Elsevier Ltd. All rights reserved.",
year = "2017",
month = feb,
day = "7",
doi = "10.1016/j.str.2016.11.023",
language = "English",
volume = "25",
pages = "231--242",
journal = "Structure",
issn = "1878-4186",
publisher = "CELL PRESS",
number = "2",

}

RIS

TY - JOUR

T1 - Crystal Structure of 4,6-α-Glucanotransferase Supports Diet-Driven Evolution of GH70 Enzymes from α-Amylases in Oral Bacteria

AU - Bai, Yuxiang

AU - Gangoiti , Joana

AU - Dijkstra, Bauke W

AU - Dijkhuizen, Lubbert

AU - Pijning, Tjaard

N1 - Copyright © 2016 Elsevier Ltd. All rights reserved.

PY - 2017/2/7

Y1 - 2017/2/7

N2 - Food processing and refining has dramatically changed the human diet, but little is known about whether this affected the evolution of enzymes in human microbiota. We present evidence that glycoside hydrolase family 70 (GH70) glucansucrases from lactobacilli, synthesizing α-glucan-type extracellular polysaccharides from sucrose, likely evolved from GH13 starch-acting α-amylases, via GH70 4,6-α-glucanotransferases. The crystal structure of a 4,6-α-glucanotransferase explains the mode of action and unique product specificity of these enzymes. While the α-amylase substrate-binding scaffold is retained, active-site loops adapted to favor transglycosylation over hydrolysis; the structure also gives clues as to how 4,6-α-glucanotransferases may have evolved further toward sucrose utilization instead of starch. Further supported by genomic, phylogenetic, and in vivo studies, we propose that dietary changes involving starch (and starch derivatives) and sucrose intake were critical factors during the evolution of 4,6-α-GTs and glucansucrases from α-amylases, allowing oral bacteria to produce extracellular polymers that contribute to biofilm formation from different substrates.

AB - Food processing and refining has dramatically changed the human diet, but little is known about whether this affected the evolution of enzymes in human microbiota. We present evidence that glycoside hydrolase family 70 (GH70) glucansucrases from lactobacilli, synthesizing α-glucan-type extracellular polysaccharides from sucrose, likely evolved from GH13 starch-acting α-amylases, via GH70 4,6-α-glucanotransferases. The crystal structure of a 4,6-α-glucanotransferase explains the mode of action and unique product specificity of these enzymes. While the α-amylase substrate-binding scaffold is retained, active-site loops adapted to favor transglycosylation over hydrolysis; the structure also gives clues as to how 4,6-α-glucanotransferases may have evolved further toward sucrose utilization instead of starch. Further supported by genomic, phylogenetic, and in vivo studies, we propose that dietary changes involving starch (and starch derivatives) and sucrose intake were critical factors during the evolution of 4,6-α-GTs and glucansucrases from α-amylases, allowing oral bacteria to produce extracellular polymers that contribute to biofilm formation from different substrates.

KW - 4,6-α-Glucanotransferase

KW - Crystal structure

KW - Starch

KW - Lactobacillus reuteri

KW - Dental caries

KW - Lactic Acid Bacteria

U2 - 10.1016/j.str.2016.11.023

DO - 10.1016/j.str.2016.11.023

M3 - Article

C2 - 28065507

VL - 25

SP - 231

EP - 242

JO - Structure

JF - Structure

SN - 1878-4186

IS - 2

ER -

ID: 38982931