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PDBsum entry 3qr3

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
3qr3
Jmol
Contents
Protein chains
329 a.a.
Ligands
SO4 ×14
Metals
_MG ×4
Waters ×523
PDB id:
3qr3
Name: Hydrolase
Title: Crystal structure of cel5a (eg2) from hypocrea jecorina (tri reesei)
Structure: Endoglucanase eg-ii. Chain: a, b. Fragment: catalytic domain. Synonym: eglii, cellulase, endo-1,4-beta-glucanase. Engineered: yes
Source: Hypocrea jecorina. Organism_taxid: 51453. Gene: cel5a, egl2. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
2.05Å     R-factor:   0.165     R-free:   0.205
Authors: T.M.Lee,M.F.Farrow,J.T.Kaiser,F.H.Arnold,S.L.Mayo
Key ref: T.M.Lee et al. (2011). A structural study of Hypocrea jecorina Cel5A. Protein Sci, 20, 1935-1940. PubMed id: 21898652 DOI: 10.1002/pro.730
Date:
16-Feb-11     Release date:   02-Nov-11    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P07982  (GUN2_HYPJE) -  Endoglucanase EG-II
Seq:
Struc:
418 a.a.
329 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   1 term 
  Biochemical function     hydrolase activity, hydrolyzing O-glycosyl compounds     1 term  

 

 
DOI no: 10.1002/pro.730 Protein Sci 20:1935-1940 (2011)
PubMed id: 21898652  
 
 
A structural study of Hypocrea jecorina Cel5A.
T.M.Lee, M.F.Farrow, F.H.Arnold, S.L.Mayo.
 
  ABSTRACT  
 
Interest in generating lignocellulosic biofuels through enzymatic hydrolysis continues to rise as nonrenewable fossil fuels are depleted. The high cost of producing cellulases, hydrolytic enzymes that cleave cellulose into fermentable sugars, currently hinders economically viable biofuel production. Here, we report the crystal structure of a prevalent endoglucanase in the biofuels industry, Cel5A from the filamentous fungus Hypocrea jecorina. The structure reveals a general fold resembling that of the closest homolog with a high-resolution structure, Cel5A from Thermoascus aurantiacus. Consistent with previously described endoglucanase structures, the H. jecorina Cel5A active site contains a primarily hydrophobic substrate binding groove and a series of hydrogen bond networks surrounding two catalytic glutamates. The reported structure, however, demonstrates stark differences between side-chain identity, loop regions, and the number of disulfides. Such structural information may aid efforts to improve the stability of this protein for industrial use while maintaining enzymatic activity through revealing nonessential and immutable regions.