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PDBsum entry 2cit

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protein ligands links
Hydrolase PDB id
2cit
Jmol
Contents
Protein chain
274 a.a. *
Ligands
G2F-BGC-BGC
Waters ×491
* Residue conservation analysis
PDB id:
2cit
Name: Hydrolase
Title: Structure of the covalent intermediate of a family 26 lichenase
Structure: Endoglucanase h. Chain: a. Fragment: residues 26-304. Synonym: egh, cellulase h, endo-1,4-beta-glucanase. Engineered: yes. Mutation: yes
Source: Clostridium thermocellum. Organism_taxid: 1515. Strain: f1/ys. Atcc: 27405. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.40Å     R-factor:   0.152     R-free:   0.179
Authors: V.A.Money,N.L.Smith,A.Scaffidi,R.V.Stick,H.J.Gilbert, G.J.Da
Key ref: V.A.Money et al. (2006). Substrate distortion by a lichenase highlights the different conformational itineraries harnessed by related glycoside hydrolases. Angew Chem Int Ed Engl, 45, 5136-5140. PubMed id: 16823793
Date:
24-Mar-06     Release date:   10-Apr-06    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P16218  (GUNH_CLOTH) -  Endoglucanase H
Seq:
Struc:
 
Seq:
Struc:
900 a.a.
274 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.3.2.1.4  - 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   2 terms 
  Biochemical function     cellulase activity     2 terms  

 

 
Angew Chem Int Ed Engl 45:5136-5140 (2006)
PubMed id: 16823793  
 
 
Substrate distortion by a lichenase highlights the different conformational itineraries harnessed by related glycoside hydrolases.
V.A.Money, N.L.Smith, A.Scaffidi, R.V.Stick, H.J.Gilbert, G.J.Davies.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19279191 R.Suzuki, Z.Fujimoto, S.Ito, S.Kawahara, S.Kaneko, K.Taira, T.Hasegawa, and A.Kuno (2009).
Crystallographic snapshots of an entire reaction cycle for a retaining xylanase from Streptomyces olivaceoviridis E-86.
  J Biochem, 146, 61-70.
PDB codes: 2d1z 2d20 2d22 2d23 2d24
18558099 D.J.Vocadlo, and G.J.Davies (2008).
Mechanistic insights into glycosidase chemistry.
  Curr Opin Chem Biol, 12, 539-555.  
18408714 L.E.Tailford, W.A.Offen, N.L.Smith, C.Dumon, C.Morland, J.Gratien, M.P.Heck, R.V.Stick, Y.Blériot, A.Vasella, H.J.Gilbert, and G.J.Davies (2008).
Structural and biochemical evidence for a boat-like transition state in beta-mannosidases.
  Nat Chem Biol, 4, 306-312.
PDB codes: 2vjx 2vl4 2vmf 2vo5 2vot 2vqt 2vqu 2vr4
18292875 V.A.Money, A.Cartmell, C.I.Guerreiro, V.M.Ducros, C.M.Fontes, H.J.Gilbert, and G.J.Davies (2008).
Probing the beta-1,3:1,4 glucanase, CtLic26A, with a thio-oligosaccharide and enzyme variants.
  Org Biomol Chem, 6, 851-853.
PDB code: 2vi0
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