The crystal structure of a hyperthermoactive exopolygalacturonase from Thermotoga maritima reveals a unique tetramer

T. Pijning; G. van Pouderoyen; L.D. Kluskens; J. van der Oost; B.W. Dijkstra

doi:10.1016/j.febslet.2009.10.047

The crystal structure of a hyperthermoactive exopolygalacturonase from Thermotoga maritima reveals a unique tetramer

T. Pijning, G. van Pouderoyen, L.D. Kluskens, J. van der Oost, B.W. Dijkstra

Research output: Contribution to journal › Article › Academic › peer-review

28 Citations (Scopus)

Abstract

The exopolygalacturonase from Thermotoga maritima is the most thermoactive and thermostable pectinase known to date. Here we present its crystal structure at 2.05A resolution. High structural homology around the active site allowed us to propose a model for substrate binding, explaining the exo-cleavage activity and specificity for non-methylated saturated galacturonate at the non-reducing end. Furthermore, the structure reveals unique features that contribute to the formation of stable tetramers in solution. Such an oligomerization has not been observed before for polygalacturonases

Original language	English
Pages (from-to)	3665-3670
Journal	FEBS Letters
Volume	583
Issue number	22
DOIs	https://doi.org/10.1016/j.febslet.2009.10.047
Publication status	Published - 2009

Keywords

active-site
endopolygalacturonase-i
aspergillus-aculeatus
sequence alignments
polygalacturonase
protein
features
crystallography
mutagenesis
family-28

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title = "The crystal structure of a hyperthermoactive exopolygalacturonase from Thermotoga maritima reveals a unique tetramer",

abstract = "The exopolygalacturonase from Thermotoga maritima is the most thermoactive and thermostable pectinase known to date. Here we present its crystal structure at 2.05A resolution. High structural homology around the active site allowed us to propose a model for substrate binding, explaining the exo-cleavage activity and specificity for non-methylated saturated galacturonate at the non-reducing end. Furthermore, the structure reveals unique features that contribute to the formation of stable tetramers in solution. Such an oligomerization has not been observed before for polygalacturonases",

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T1 - The crystal structure of a hyperthermoactive exopolygalacturonase from Thermotoga maritima reveals a unique tetramer

AU - Pijning, T.

AU - van Pouderoyen, G.

AU - Kluskens, L.D.

AU - van der Oost, J.

AU - Dijkstra, B.W.

PY - 2009

Y1 - 2009

N2 - The exopolygalacturonase from Thermotoga maritima is the most thermoactive and thermostable pectinase known to date. Here we present its crystal structure at 2.05A resolution. High structural homology around the active site allowed us to propose a model for substrate binding, explaining the exo-cleavage activity and specificity for non-methylated saturated galacturonate at the non-reducing end. Furthermore, the structure reveals unique features that contribute to the formation of stable tetramers in solution. Such an oligomerization has not been observed before for polygalacturonases

AB - The exopolygalacturonase from Thermotoga maritima is the most thermoactive and thermostable pectinase known to date. Here we present its crystal structure at 2.05A resolution. High structural homology around the active site allowed us to propose a model for substrate binding, explaining the exo-cleavage activity and specificity for non-methylated saturated galacturonate at the non-reducing end. Furthermore, the structure reveals unique features that contribute to the formation of stable tetramers in solution. Such an oligomerization has not been observed before for polygalacturonases

KW - active-site

KW - endopolygalacturonase-i

KW - aspergillus-aculeatus

KW - sequence alignments

KW - polygalacturonase

KW - protein

KW - features

KW - crystallography

KW - mutagenesis

KW - family-28

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DO - 10.1016/j.febslet.2009.10.047

M3 - Article

SN - 0014-5793

VL - 583

SP - 3665

EP - 3670

JO - FEBS Letters

JF - FEBS Letters

IS - 22

ER -

The crystal structure of a hyperthermoactive exopolygalacturonase from Thermotoga maritima reveals a unique tetramer

Abstract

Keywords

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