PDBsum entry 1k72

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
Protein chains
612 a.a. *
GOL ×2
_CA ×4
_MG ×4
Waters ×765
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: The x-ray crystal structure of cel9g complexed with cellotri
Structure: Endoglucanase 9g. Chain: a, b. Engineered: yes
Source: Clostridium cellulolyticum. Organism_taxid: 1521. Gene: celccg. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
1.80Å     R-factor:   0.166     R-free:   0.198
Authors: D.Mandelman,A.Belaich,J.P.Belaich,N.Aghajari,H.Driguez,R.Has
Key ref: D.Mandelman et al. (2003). X-Ray crystal structure of the multidomain endoglucanase Cel9G from Clostridium cellulolyticum complexed with natural and synthetic cello-oligosaccharides. J Bacteriol, 185, 4127-4135. PubMed id: 12837787
18-Oct-01     Release date:   15-Jul-03    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P37700  (GUNG_CLOCE) -  Endoglucanase G
725 a.a.
612 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.  - Cellulase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endohydrolysis of 1,4-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     carbohydrate metabolic process   1 term 
  Biochemical function     catalytic activity     4 terms  


J Bacteriol 185:4127-4135 (2003)
PubMed id: 12837787  
X-Ray crystal structure of the multidomain endoglucanase Cel9G from Clostridium cellulolyticum complexed with natural and synthetic cello-oligosaccharides.
D.Mandelman, A.Belaich, J.P.Belaich, N.Aghajari, H.Driguez, R.Haser.
Complete cellulose degradation is the first step in the use of biomass as a source of renewable energy. To this end, the engineering of novel cellulase activity, the activity responsible for the hydrolysis of the beta-1,4-glycosidic bonds in cellulose, is a topic of great interest. The high-resolution X-ray crystal structure of a multidomain endoglucanase from Clostridium cellulolyticum has been determined at a 1.6-A resolution. The endoglucanase, Cel9G, is comprised of a family 9 catalytic domain attached to a family III(c) cellulose-binding domain. The two domains together form a flat platform onto which crystalline cellulose is suggested to bind and be fed into the active-site cleft for endolytic hydrolysis. To further dissect the structural basis of cellulose binding and hydrolysis, the structures of Cel9G in the presence of cellobiose, cellotriose, and a DP-10 thio-oligosaccharide inhibitor were resolved at resolutions of 1.7, 1.8, and 1.9 A, respectively.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21098515 Y.Honda, N.Shimaya, K.Ishisaki, M.Ebihara, and H.Taniguchi (2011).
Elucidation of exo-{beta}-D-glucosaminidase activity of a family 9 glycoside hydrolase (PBPRA0520) from Photobacterium profundum SS9.
  Glycobiology, 21, 503-511.  
20159465 N.M.Koropatkin, and T.J.Smith (2010).
SusG: a unique cell-membrane-associated alpha-amylase from a prominent human gut symbiont targets complex starch molecules.
  Structure, 18, 200-215.
PDB codes: 3k8k 3k8l 3k8m
17905885 F.Mingardon, A.Chanal, C.Tardif, E.A.Bayer, and H.P.Fierobe (2007).
Exploration of new geometries in cellulosome-like chimeras.
  Appl Environ Microbiol, 73, 7138-7149.  
17209020 J.C.Blouzard, C.Bourgeois, Philip, O.Valette, A.Bélaïch, C.Tardif, J.P.Bélaïch, and S.Pagès (2007).
Enzyme diversity of the cellulolytic system produced by Clostridium cellulolyticum explored by two-dimensional analysis: identification of seven genes encoding new dockerin-containing proteins.
  J Bacteriol, 189, 2300-2309.  
17022659 M.Desvaux (2006).
Unravelling carbon metabolism in anaerobic cellulolytic bacteria.
  Biotechnol Prog, 22, 1229-1238.  
16917793 V.L.Yip, and S.G.Withers (2006).
Family 4 glycosidases carry out efficient hydrolysis of thioglycosides by an alpha,beta-elimination mechanism.
  Angew Chem Int Ed Engl, 45, 6179-6182.  
16102601 M.Desvaux (2005).
Clostridium cellulolyticum: model organism of mesophilic cellulolytic clostridia.
  FEMS Microbiol Rev, 29, 741-764.  
15604820 L.Hildén, and G.Johansson (2004).
Recent developments on cellulases and carbohydrate-binding modules with cellulose affinity.
  Biotechnol Lett, 26, 1683-1693.  
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