PDBsum entry 1vrx

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protein Protein-protein interface(s) links
Hydrolase PDB id
Protein chains
358 a.a. *
Waters ×232
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Endocellulase e1 from acidothermus cellulolyticus mutant y245g
Structure: Endocellulase e1 from a. Cellulolyticus. Chain: a, b. Fragment: catalytic domain, bamh1 fragment. Engineered: yes. Mutation: yes
Source: Acidothermus cellulolyticus. Organism_taxid: 28049. Expressed in: escherichia coli. Expression_system_taxid: 562
2.40Å     R-factor:   0.193     R-free:   0.254
Authors: J.O.Baker,J.R.Mccarley,R.Lovett,C.H.Yu,W.S.Adney, T.R.Rignall,T.B.Vinzant,S.R.Decker,J.Sakon,M.E.Himmel
Key ref: J.O.Baker et al. (2005). Catalytically enhanced endocellulase Cel5A from Acidothermus cellulolyticus. Appl Biochem Biotechnol, 121, 129-148. PubMed id: 15917594
30-Jun-05     Release date:   05-Jul-05    
Supersedes: 1c0d
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P54583  (GUN1_ACIC1) -  Endoglucanase E1
562 a.a.
358 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!
  Biological process     carbohydrate metabolic process   1 term 
  Biochemical function     hydrolase activity, hydrolyzing O-glycosyl compounds     1 term  


Appl Biochem Biotechnol 121:129-148 (2005)
PubMed id: 15917594  
Catalytically enhanced endocellulase Cel5A from Acidothermus cellulolyticus.
J.O.Baker, J.R.McCarley, R.Lovett, C.H.Yu, W.S.Adney, T.R.Rignall, T.B.Vinzant, S.R.Decker, J.Sakon, M.E.Himmel.
<When Tyr245 in endocellulase Cel5A from Acidothermus cellulolyticus was changed to Gly (Y245G) by designed mutation, the value of Ki for inhibition of the enzyme by the product cellobiose was increased more than 1480%. This reduction in product inhibition enabled the mutant enzyme (used in conjunction with Trichoderma reesei cellobiohydrolase-I) to release soluble sugars from biomass cellulose at a rate as much as 40% greater than that achieved by the wild-type (WT) enzyme. The mutant was designed on the basis of the previously published crystal structure of the WT enzyme/substrate complex (at a resolution of 2.4 A), which provided insights into the enzyme mechanism at the atomic level and identified Tyr245 as a key residue interacting with a leaving group. To determine the origin of the change in activity, the crystal structure of Y245G was solved at 2.4-A resolution to an R-factor of 0.19 (R-free = 0.25). To obtain additional information on the enzyme-product interactions, density functional calculations were performed on representative fragments of the WT Cel5A and Y245G. The combined results indicate that the loss of the platform (Y245G) and of a hydrogen bond (from a conformational change in Gln247) reduces the binding energy between product and enzyme by several kilo calories per mole. Both kinetic and structural analyses thus relate the increased enzymatic activity to reduced product inhibition.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20803139 C.Liang, Y.Xue, M.Fioroni, F.Rodríguez-Ropero, C.Zhou, U.Schwaneberg, and Y.Ma (2011).
Cloning and characterization of a thermostable and halo-tolerant endoglucanase from Thermoanaerobacter tengcongensis MB4.
  Appl Microbiol Biotechnol, 89, 315-326.  
  19680472 M.Maki, K.T.Leung, and W.Qin (2009).
The prospects of cellulase-producing bacteria for the bioconversion of lignocellulosic biomass.
  Int J Biol Sci, 5, 500-516.  
19148633 S.P.Voutilainen, H.Boer, M.Alapuranen, J.Jänis, J.Vehmaanperä, and A.Koivula (2009).
Improving the thermostability and activity of Melanocarpus albomyces cellobiohydrolase Cel7B.
  Appl Microbiol Biotechnol, 83, 261-272.  
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