PDBsum entry 2bod

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Hydrolase PDB id
Jmol PyMol
Protein chain
279 a.a. *
Waters ×225
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Catalytic domain of endo-1,4-glucanase cel6a from thermobifida fusca in complex with methyl cellobiosyl-4- thio-beta-cellobioside
Structure: Endoglucanase e-2. Chain: x. Fragment: catalytic domain, residues 32-317. Synonym: endo-1,4-beta-glucanase e-2, cellulase e-2, cellulase e2. Engineered: yes
Source: Thermomonospora fusca. Organism_taxid: 2021. Atcc: 27730. Expressed in: escherichia coli. Expression_system_taxid: 469008.
1.5Å     R-factor:   0.186     R-free:   0.214
Authors: A.M.Larsson,T.Bergfors,E.Dultz,D.C.Irwin,A.Roos,H.Driguez, D.B.Wilson,T.A.Jones
Key ref:
A.M.Larsson et al. (2005). Crystal structure of Thermobifida fusca endoglucanase Cel6A in complex with substrate and inhibitor: the role of tyrosine Y73 in substrate ring distortion. Biochemistry, 44, 12915-12922. PubMed id: 16185060 DOI: 10.1021/bi0506730
10-Apr-05     Release date:   05-Oct-05    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P26222  (GUN2_THEFU) -  Endoglucanase E-2
441 a.a.
279 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     cellulose catabolic process   1 term 
  Biochemical function     hydrolase activity, hydrolyzing O-glycosyl compounds     1 term  


DOI no: 10.1021/bi0506730 Biochemistry 44:12915-12922 (2005)
PubMed id: 16185060  
Crystal structure of Thermobifida fusca endoglucanase Cel6A in complex with substrate and inhibitor: the role of tyrosine Y73 in substrate ring distortion.
A.M.Larsson, T.Bergfors, E.Dultz, D.C.Irwin, A.Roos, H.Driguez, D.B.Wilson, T.A.Jones.
Endoglucanase Cel6A from Thermobifida fusca hydrolyzes the beta-1,4 linkages in cellulose at accessible points along the polymer. The structure of the catalytic domain of Cel6A from T. fusca in complex with a nonhydrolysable substrate analogue that acts as an inhibitor, methylcellobiosyl-4-thio-beta-cellobioside (Glc(2)-S-Glc(2)), has been determined to 1.5 A resolution. The glycosyl unit in subsite -1 was sterically hindered by Tyr73 and forced into a distorted (2)S(o) conformation. In the enzyme where Tyr73 was mutated to a serine residue, the hindrance was removed and the glycosyl unit in subsite -1 had a relaxed (4)C(1) chair conformation. The relaxed conformation was seen in two complex structures of the mutated enzyme, with cellotetrose (Glc(4)) at 1.64 A and Glc(2)-S-Glc(2) at 1.04 A resolution.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21273341 D.W.Cockburn, and A.J.Clarke (2011).
Modulating the pH-activity profile of cellulase A from Cellulomonas fimi by replacement of surface residues.
  Protein Eng Des Sel, 24, 429-437.  
20127424 D.B.Jordan, and J.D.Braker (2010).
beta-D-Xylosidase from Selenomonas ruminantium: role of glutamate 186 in catalysis revealed by site-directed mutagenesis, alternate substrates, and active-site inhibitor.
  Appl Biochem Biotechnol, 161, 395-410.  
19435780 C.E.McGrath, T.V.Vuong, and D.B.Wilson (2009).
Site-directed mutagenesis to probe catalysis by a Thermobifida fusca beta-1,3-glucanase (Lam81A).
  Protein Eng Des Sel, 22, 375-382.  
19523117 T.V.Vuong, and D.B.Wilson (2009).
The absence of an identifiable single catalytic base residue in Thermobifida fusca exocellulase Cel6B.
  FEBS J, 276, 3837-3845.  
18832174 E.J.Dimise, P.F.Widboom, and S.D.Bruner (2008).
Structure elucidation and biosynthesis of fuscachelins, peptide siderophores from the moderate thermophile Thermobifida fusca.
  Proc Natl Acad Sci U S A, 105, 15311-15316.  
17724729 B.Mertz, A.D.Hill, C.Mulakala, and P.J.Reilly (2007).
Automated docking to explore subsite binding by glycoside hydrolase family 6 cellobiohydrolases and endoglucanases.
  Biopolymers, 87, 249-260.  
17468286 F.Mingardon, A.Chanal, A.M.López-Contreras, C.Dray, E.A.Bayer, and H.P.Fierobe (2007).
Incorporation of fungal cellulases in bacterial minicellulosomes yields viable, synergistically acting cellulolytic complexes.
  Appl Environ Microbiol, 73, 3822-3832.  
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