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

The exopolygalacturonase from Thermotoga maritima is the most thermoactive and thermostable pectinase known to date. Here we present its crystal structure at 2.05Å resolution. High structural homology around the active site allowed us to propose a model for substrate binding, explaining the exo-clea...

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Bibliographic Details
Published in:FEBS letters 2009-11, Vol.583 (22), p.3665-3670
Main Authors: Pijning, Tjaard, van Pouderoyen, Gertie, Kluskens, Leon, van der Oost, John, Dijkstra, Bauke W.
Format: Article
Language:English
Subjects:
4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid
active-site
aspergillus-aculeatus
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
BES
Catalytic Domain
Crystal structure
Crystallization
crystallography
Crystallography, X-Ray
DLS
dynamic light scattering
endopolygalacturonase-i
Exopolygalacturonase
family-28
features
Glycoside Hydrolases - chemistry
Glycoside Hydrolases - metabolism
glycosyl hydrolase
HEPES
Hexuronic Acids - chemistry
Hexuronic Acids - metabolism
Hot Temperature
Models, Molecular
molecular weight
mutagenesis
N,N-bis(2-hydroxyethyl)-2-aminoethanesulfonic acid
Oligomerization
PEG
polyethylene glycol
polygalacturonase
protein
Protein Binding
Protein Multimerization
Protein Structure, Quaternary
Protein Structure, Secondary
Protein Structure, Tertiary
R.M.S.D
root mean square deviation
sequence alignments
Stereum purpureum
Substrate Specificity
Thermostability
Thermotoga maritima
Thermotoga maritima - enzymology
X-ray crystallography
Yersinia enterocolitica
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Description
Summary:The exopolygalacturonase from Thermotoga maritima is the most thermoactive and thermostable pectinase known to date. Here we present its crystal structure at 2.05Å 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.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2009.10.047