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PDBsum entry 3jur
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Contents |
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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The crystal structure of a hyperthermoactive exopolygalacturonase from thermotoga maritima
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Structure:
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Exo-poly-alpha-d-galacturonosidase. Chain: a, b, c, d. Engineered: yes
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Source:
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Thermotoga maritima. Organism_taxid: 2336. Strain: msb8(dsm3109). Gene: tm0437. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.05Å
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R-factor:
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0.177
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R-free:
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0.220
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Authors:
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T.Pijning,G.Van Pouderoyen,L.D.Kluskens,J.Van Der Oost,B.W.Dijkstra
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Key ref:
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T.Pijning
et al.
(2009).
The crystal structure of a hyperthermoactive exopolygalacturonase from Thermotoga maritima reveals a unique tetramer.
Febs Lett,
583,
3665-3670.
PubMed id:
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Date:
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15-Sep-09
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Release date:
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17-Nov-09
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PROCHECK
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Headers
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References
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Q9WYR8
(Q9WYR8_THEMA) -
Exo-poly-alpha-D-galacturonosidase, putative from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
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Seq:
Struc:
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448 a.a.
444 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Enzyme class:
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E.C.3.2.1.15
- endo-polygalacturonase.
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Reaction:
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(1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m
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(1,4-alpha-D-galacturonosyl)n+m
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+
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H2O
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=
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(1,4-alpha-D-galacturonosyl)n
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+
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(1,4-alpha-D-galacturonosyl)m
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Febs Lett
583:3665-3670
(2009)
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PubMed id:
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The crystal structure of a hyperthermoactive exopolygalacturonase from Thermotoga maritima reveals a unique tetramer.
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T.Pijning,
G.van Pouderoyen,
L.Kluskens,
J.van der Oost,
B.W.Dijkstra.
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ABSTRACT
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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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Links
