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Title: The Structural Basis of Exopolygalacturonase Activity in a Family 28 Glycoside Hydrolase

Abstract

Family 28 glycoside hydrolases (polygalacturonases) are found in organisms across the plant, fungal and bacterial kingdoms, where they are central to diverse biological functions such as fruit ripening, biomass recycling and plant pathogenesis. The structures of several polygalacturonases have been reported; however, all of these enzymes utilize an endo-mode of digestion, which generates a spectrum of oligosaccharide products with varying degrees of polymerization. The structure of a complementary exo-acting polygalacturonase and an accompanying explanation of the molecular determinants for its specialized activity have been noticeably lacking. We present the structure of an exopolygalacturonase from Yersinia enterocolitica, YeGH28 in a native form (solved to 2.19 {angstrom} resolution) and a digalacturonic acid product complex (solved to 2.10 {angstrom} resolution). The activity of YeGH28 is due to inserted stretches of amino acid residues that transform the active site from the open-ended channel observed in the endopolygalacturonases to a closed pocket that restricts the enzyme to the exclusive attack of the non-reducing end of oligogalacturonide substrates. In addition, YeGH28 possesses a fused FN3 domain with unknown function, the first such structure described in pectin active enzymes.

Authors:
;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
929882
Report Number(s):
BNL-80454-2008-JA
Journal ID: ISSN 0022-2836; JMOBAK; TRN: US200822%%1067
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Journal of Molecular Biology; Journal Volume: 368
Country of Publication:
United States
Language:
English
Subject:
09 BIOMASS FUELS; AMINO ACIDS; BIOLOGICAL FUNCTIONS; BIOMASS; DIGESTION; ENZYMES; FRUITS; GLYCOSIDES; HYDROLASES; OLIGOSACCHARIDES; PATHOGENESIS; PECTINS; PLANTS; POLYMERIZATION; RECYCLING; RESIDUES; RESOLUTION; RIPENING; SUBSTRATES; national synchrotron light source

Citation Formats

Abbott,D., and Boraston, A. The Structural Basis of Exopolygalacturonase Activity in a Family 28 Glycoside Hydrolase. United States: N. p., 2007. Web. doi:10.1016/j.jmb.2007.02.083.
Abbott,D., & Boraston, A. The Structural Basis of Exopolygalacturonase Activity in a Family 28 Glycoside Hydrolase. United States. doi:10.1016/j.jmb.2007.02.083.
Abbott,D., and Boraston, A. Mon . "The Structural Basis of Exopolygalacturonase Activity in a Family 28 Glycoside Hydrolase". United States. doi:10.1016/j.jmb.2007.02.083.
@article{osti_929882,
title = {The Structural Basis of Exopolygalacturonase Activity in a Family 28 Glycoside Hydrolase},
author = {Abbott,D. and Boraston, A.},
abstractNote = {Family 28 glycoside hydrolases (polygalacturonases) are found in organisms across the plant, fungal and bacterial kingdoms, where they are central to diverse biological functions such as fruit ripening, biomass recycling and plant pathogenesis. The structures of several polygalacturonases have been reported; however, all of these enzymes utilize an endo-mode of digestion, which generates a spectrum of oligosaccharide products with varying degrees of polymerization. The structure of a complementary exo-acting polygalacturonase and an accompanying explanation of the molecular determinants for its specialized activity have been noticeably lacking. We present the structure of an exopolygalacturonase from Yersinia enterocolitica, YeGH28 in a native form (solved to 2.19 {angstrom} resolution) and a digalacturonic acid product complex (solved to 2.10 {angstrom} resolution). The activity of YeGH28 is due to inserted stretches of amino acid residues that transform the active site from the open-ended channel observed in the endopolygalacturonases to a closed pocket that restricts the enzyme to the exclusive attack of the non-reducing end of oligogalacturonide substrates. In addition, YeGH28 possesses a fused FN3 domain with unknown function, the first such structure described in pectin active enzymes.},
doi = {10.1016/j.jmb.2007.02.083},
journal = {Journal of Molecular Biology},
number = ,
volume = 368,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}