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PDBsum entry 3acf
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Hydrolase
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Title:
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Crystal structure of carbohydrate-binding module family 28 from clostridium josui cel5a in a ligand-free form
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Structure:
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Beta-1,4-endoglucanase. Chain: a. Fragment: unp residues 560-752. Synonym: carbohydrate-binding module family 28. Engineered: yes
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Source:
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Clostridium josui. Organism_taxid: 1499. Gene: cela. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.60Å
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R-factor:
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0.158
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R-free:
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0.191
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Authors:
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K.Tsukimoto,R.Takada,Y.Araki,K.Suzuki,S.Karita,T.Wakagi,H.Shoun, T.Watanabe,S.Fushinobu
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Key ref:
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K.Tsukimoto
et al.
(2010).
Recognition of cellooligosaccharides by a family 28 carbohydrate-binding module.
Febs Lett,
584,
1205-1211.
PubMed id:
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Date:
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04-Jan-10
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Release date:
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02-Mar-10
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PROCHECK
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Headers
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References
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Q59290
(Q59290_RUMJO) -
Beta-1,4-endoglucanase from Ruminiclostridium josui
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Seq:
Struc:
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930 a.a.
193 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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Enzyme class:
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E.C.3.2.1.4
- cellulase.
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Reaction:
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Endohydrolysis of 1,4-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
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Febs Lett
584:1205-1211
(2010)
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PubMed id:
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Recognition of cellooligosaccharides by a family 28 carbohydrate-binding module.
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K.Tsukimoto,
R.Takada,
Y.Araki,
K.Suzuki,
S.Karita,
T.Wakagi,
H.Shoun,
T.Watanabe,
S.Fushinobu.
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ABSTRACT
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The crystal structures of a carbohydrate-binding module (CBM) family 28 domain
of endoglucanase Cel5A from Clostridium josui have been determined in
ligand-free and complex forms with cellobiose, cellotetraose, and cellopentaose
as the first complex structures of this family. In the cleft of a beta-sandwich
fold, the ligands are recognized by stacking interactions and hydrogen bonds.
Conformations of the bound cellooligosaccharides are similar to those in
crystals and solution but clearly different from the cellulose structure.
Interestingly, the glucan chain bound on CBM28 is in the opposite direction of
that bound to CBM17, although these families share significant structural
similarity.
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Links
