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PDBsum entry 3mmu
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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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Crystal structure of endoglucanase cel5a from the hyperthermophilic thermotoga maritima
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Structure:
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Endoglucanase. Chain: a, b, c, d, e, f, g, h. Synonym: endoglucanase cel5a. Engineered: yes
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Source:
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Thermotoga maritima. Organism_taxid: 2336. Gene: tm_1751. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.20Å
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R-factor:
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0.206
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R-free:
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0.218
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Authors:
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J.H.Pereira,Z.Chen,R.P.Mcandrew,R.Sapra,S.R.Chhabra,K.L.Sale, B.A.Simmons,P.D.Adams
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Key ref:
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J.H.Pereira
et al.
(2010).
Biochemical characterization and crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima.
J Struct Biol,
172,
372-379.
PubMed id:
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Date:
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20-Apr-10
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Release date:
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28-Jul-10
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PROCHECK
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Headers
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References
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Q9X273
(Q9X273_THEMA) -
Endoglucanase from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
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Seq:
Struc:
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317 a.a.
309 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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J Struct Biol
172:372-379
(2010)
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PubMed id:
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Biochemical characterization and crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima.
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J.H.Pereira,
Z.Chen,
R.P.McAndrew,
R.Sapra,
S.R.Chhabra,
K.L.Sale,
B.A.Simmons,
P.D.Adams.
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ABSTRACT
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Tm_Cel5A, which belongs to family 5 of the glycoside hydrolases, is an extremely
stable enzyme among the endo-acting glycosidases present in the
hyperthermophilic organism Thermotoga maritima. Members of GH5 family shows a
common (beta/alpha)(8) TIM-barrel fold in which the catalytic acid/base and
nucleophile are located on strands beta-4 and beta-7 of the barrel fold.
Thermally resistant cellulases are desirable for lignocellulosic biofuels
production and the Tm_Cel5A is an excellent candidate for use in the degradation
of polysaccharides present on biomass. This paper describes two Tm_Cel5A
structures (crystal forms I and II) solved at 2.20 and 1.85 A resolution,
respectively. Our analyses of the Tm_Cel5A structure and comparison to a
mesophilic GH5 provides a basis for the thermostability associated with
Tm_Cel5A. Furthermore, both crystal forms of Tm_Cel5A possess a cadmium (Cd(2+))
ion bound between the two catalytic residues. Activity assays of Tm_Cel5A
confirmed a strong inhibition effect in the presence of Cd(2+) metal ions
demonstrating competition with the natural substrate for the active site. Based
on the structural information we have obtained for Tm_Cel5A, protein
bioengineering can be used to potentially increase the thermostability of
mesophilic cellulase enzymes.
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Links
