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PDBsum entry 4bmf

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protein links
Hydrolase PDB id
4bmf
Jmol
Contents
Protein chain
38 a.a.
PDB id:
4bmf
Name: Hydrolase
Title: Solution structure of the cellulose-binding domain of endoglucanase i from trichoderma reesei and its interaction with cello-oligosaccharides
Structure: Endoglucanase eg-1. Chain: a. Fragment: cellulose-binding domain, residues 422-459. Synonym: endoglucanase i, cellulase, endo-1,4-beta-glucanas ec: 3.2.1.4
Source: Synthetic: yes. Hypocrea jecorina. Organism_taxid: 51453
NMR struc: 19 models
Authors: M.L.Mattinen,M.Linder,T.Drakenberg,A.Annila
Key ref: M.L.Mattinen et al. (1998). Solution structure of the cellulose-binding domain of endoglucanase I from Trichoderma reesei and its interaction with cello-oligosaccharides. Eur J Biochem, 256, 279-286. PubMed id: 9760165
Date:
08-May-13     Release date:   22-May-13    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P07981  (GUN1_HYPJE) -  Endoglucanase EG-1
Seq:
Struc:
459 a.a.
38 a.a.
Key:    PfamA domain  Secondary structure

 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!
  Cellular component     extracellular region   1 term 
  Biological process     carbohydrate metabolic process   1 term 
  Biochemical function     hydrolase activity, hydrolyzing O-glycosyl compounds     2 terms  

 

 
Eur J Biochem 256:279-286 (1998)
PubMed id: 9760165  
 
 
Solution structure of the cellulose-binding domain of endoglucanase I from Trichoderma reesei and its interaction with cello-oligosaccharides.
M.L.Mattinen, M.Linder, T.Drakenberg, A.Annila.
 
  ABSTRACT  
 
The solution structure of a synthetic 38-residue cellulose-binding domain (CBD) of endoglucanase I from Trichoderma reesei (CBD(EGI)) was determined by two-dimensional 1H-NMR spectroscopy. 100 structures were generated from a total of 599 NOE derived distance restraints and 28 phi and 14 chi dihedral angle restraints. For the final set of 19 selected structures, the rms deviation about the mean structure was 0.83+/-0.26 A for all atoms and 0.50+/-0.22 A for the backbone atoms. The structure of CBD(EGI) was very similar to that of CBD of cellobiohydrolase I from T reesei (CBD(CBHI)). The backbone trace of CBD(EGI) followed closely the irregular triple-stranded antiparallel beta-sheet structure of CBD(CBHI). Moreover, apart from the different side chains of Trp7 (CBD(EGI)) and Tyr5 (CBD(CBHI)), the cellulose-binding face of CBD(EGI) was similar to that of CBD(CBHI) within the precision of the structures. Finally, the interaction between CBD(EGI) and soluble sugars was investigated using cellopentaose and cellohexaose as substrates. Experiments showed that the interactions between CBD(EGI) and cellobiose units of sugars are specific, supporting the previously presented model for the CBD binding to crystalline cellulose.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
  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.  
  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
  10788483 T.Ikegami, T.Okada, M.Hashimoto, S.Seino, T.Watanabe, and M.Shirakawa (2000).
Solution structure of the chitin-binding domain of Bacillus circulans WL-12 chitinase A1.
  J Biol Chem, 275, 13654-13661.
PDB code: 1ed7
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.