PDBsum entry 1cx1

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protein links
Hydrolase PDB id
Protein chain
153 a.a. *
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Second n-terminal cellulose-binding domain from cellulomonas fimi beta-1,4-glucanasE C, nmr, 22 structures
Structure: EndoglucanasE C. Chain: a. Fragment: residues 176-328. Engineered: yes
Source: Cellulomonas fimi. Organism_taxid: 1708. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 22 models
Authors: E.Brun,P.E.Johnson,L.A.Creagh,C.A.Haynes,P.Tomme,P.Webster, D.G Kilburn,L.P.Mcintosh
Key ref:
E.Brun et al. (2000). Structure and binding specificity of the second N-terminal cellulose-binding domain from Cellulomonas fimi endoglucanase C. Biochemistry, 39, 2445-2458. PubMed id: 10704194 DOI: 10.1021/bi992079u
27-Aug-99     Release date:   02-Apr-00    
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Protein chain
Pfam   ArchSchema ?
P14090  (GUNC_CELFA) -  Endoglucanase C
1101 a.a.
153 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 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!
  Biochemical function     hydrolase activity, acting on glycosyl bonds     1 term  


DOI no: 10.1021/bi992079u Biochemistry 39:2445-2458 (2000)
PubMed id: 10704194  
Structure and binding specificity of the second N-terminal cellulose-binding domain from Cellulomonas fimi endoglucanase C.
E.Brun, P.E.Johnson, A.L.Creagh, P.Tomme, P.Webster, C.A.Haynes, L.P.McIntosh.
The 1,4-beta-glucanase CenC from Cellulomonas fimi contains two cellulose-binding domains, CBD(N1) and CBD(N2), arranged in tandem at its N-terminus. These homologous CBDs are distinct in their selectivity for binding amorphous and not crystalline cellulose. Multidimensional heteronuclear nuclear magnetic resonance (NMR) spectroscopy was used to determine the tertiary structure of CBD(N2) in the presence of saturating amounts of cellopentaose. A total of 1996 experimental restraints were used to calculate an ensemble of 21 final structures for the protein. CBD(Nu2) is composed of 11 beta-strands, folded into two antiparallel beta-sheets, with a topology of a jellyroll beta-sandwich. On the basis of patterns of chemical shift perturbations accompanying the addition of cellooligosaccharides, as well as the observation of intermolecular protein-sugar NOE interactions, the cellulose-binding site of CBD(N2) was identified as a cleft that lies across one face of the beta-sandwich. The thermodynamic basis for the binding of cellooligosaccharides was investigated using isothermal titration calorimetry and NMR spectroscopy. Binding is enthalpically driven and consistent with a structural model involving hydrogen bonding between the equatorial hydroxyls of the glucopyranosyl rings and polar amino acid side chains lining the CBD(N2) cleft. Affinity electrophoresis was used to determine that CBD(N2) also binds soluble beta-1,4-linked polymers of glucose, including hydroxyethylcellulose and beta-1,3-1,4-glucans. This study complements a previous analysis of CBD(N1) [Johnson, P. E., Joshi, M. D., Tomme, P., Kilburn, D. G., and McIntosh, L. P. (1996) Biochemistry 35, 14381-14394] and demonstrates that the homologous CBDs from CenC share very similar structures and sugar binding properties.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21290602 D.M.Kim, M.Umetsu, K.Takai, T.Matsuyama, N.Ishida, H.Takahashi, R.Asano, and I.Kumagai (2011).
Enhancement of cellulolytic enzyme activity by clustering cellulose binding domains on nanoscaffolds.
  Small, 7, 656-664.  
15010454 V.M.Pires, J.L.Henshaw, J.A.Prates, D.N.Bolam, L.M.Ferreira, C.M.Fontes, B.Henrissat, A.Planas, H.J.Gilbert, and M.Czjzek (2004).
The crystal structure of the family 6 carbohydrate binding module from Cellvibrio mixtus endoglucanase 5a in complex with oligosaccharides reveals two distinct binding sites with different ligand specificities.
  J Biol Chem, 279, 21560-21568.
PDB codes: 1uxx 1uxz 1uy0 1uyx 1uyy 1uyz 1uz0
12833544 D.J.Rigden, and M.J.Jedrzejas (2003).
Genome-based identification of a carbohydrate binding module in Streptococcus pneumoniae hyaluronate lyase.
  Proteins, 52, 203-211.  
11980475 P.J.Simpson, S.J.Jamieson, M.Abou-Hachem, E.N.Karlsson, H.J.Gilbert, O.Holst, and M.P.Williamson (2002).
The solution structure of the CBM4-2 carbohydrate binding module from a thermostable Rhodothermus marinus xylanase.
  Biochemistry, 41, 5712-5719.
PDB codes: 1k42 1k45
12391332 S.J.Charnock, D.N.Bolam, D.Nurizzo, L.Szabó, V.A.McKie, H.J.Gilbert, and G.J.Davies (2002).
Promiscuity in ligand-binding: The three-dimensional structure of a Piromyces carbohydrate-binding module, CBM29-2, in complex with cello- and mannohexaose.
  Proc Natl Acad Sci U S A, 99, 14077-14082.
PDB codes: 1gwk 1gwl 1gwm
11371185 A.B.Boraston, A.L.Creagh, M.M.Alam, J.M.Kormos, P.Tomme, C.A.Haynes, R.A.Warren, and D.G.Kilburn (2001).
Binding specificity and thermodynamics of a family 9 carbohydrate-binding module from Thermotoga maritima xylanase 10A.
  Biochemistry, 40, 6240-6247.  
11560933 A.C.Freelove, D.N.Bolam, P.White, G.P.Hazlewood, and H.J.Gilbert (2001).
A novel carbohydrate-binding protein is a component of the plant cell wall-degrading complex of Piromyces equi.
  J Biol Chem, 276, 43010-43017.  
11327868 D.N.Bolam, H.Xie, P.White, P.J.Simpson, S.M.Hancock, M.P.Williamson, and H.J.Gilbert (2001).
Evidence for synergy between family 2b carbohydrate binding modules in Cellulomonas fimi xylanase 11A.
  Biochemistry, 40, 2468-2477.
PDB codes: 1heh 1hej
11160085 I.A.Kataeva, R.D.Seidel, X.L.Li, and L.G.Ljungdahl (2001).
Properties and mutation analysis of the CelK cellulose-binding domain from the Clostridium thermocellum cellulosome.
  J Bacteriol, 183, 1552-1559.  
11378487 J.R.Mielenz (2001).
Ethanol production from biomass: technology and commercialization status.
  Curr Opin Microbiol, 4, 324-329.  
  11673472 M.Czjzek, D.N.Bolam, A.Mosbah, J.Allouch, C.M.Fontes, L.M.Ferreira, O.Bornet, V.Zamboni, H.Darbon, N.L.Smith, G.W.Black, B.Henrissat, and H.J.Gilbert (2001).
The location of the ligand-binding site of carbohydrate-binding modules that have evolved from a common sequence is not conserved.
  J Biol Chem, 276, 48580-48587.
PDB code: 1gmm
11371186 V.Notenboom, A.B.Boraston, D.G.Kilburn, and D.R.Rose (2001).
Crystal structures of the family 9 carbohydrate-binding module from Thermotoga maritima xylanase 10A in native and ligand-bound forms.
  Biochemistry, 40, 6248-6256.
PDB codes: 1i82 1i8a 1i8u
10913296 J.Kormos, P.E.Johnson, E.Brun, P.Tomme, L.P.McIntosh, C.A.Haynes, and D.G.Kilburn (2000).
Binding site analysis of cellulose binding domain CBD(N1) from endoglucanse C of Cellulomonas fimi by site-directed mutagenesis.
  Biochemistry, 39, 8844-8852.  
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