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PDBsum entry 3gbs

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protein links
Hydrolase PDB id
3gbs
Jmol
Contents
Protein chain
187 a.a. *
Waters ×269
* Residue conservation analysis
PDB id:
3gbs
Name: Hydrolase
Title: Crystal structure of aspergillus oryzae cutinase
Structure: Cutinase 1. Chain: a. Fragment: unp residues 17-213. Synonym: cutin hydrolase 1, l1. Engineered: yes
Source: Aspergillus oryzae. Organism_taxid: 5062. Strain: ifo 4202. Gene: ao090005000029, cutl. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
Resolution:
1.75Å     R-factor:   0.194     R-free:   0.199
Authors: Y.Gosser,Z.Lu,G.Alemu,H.Li,X.Kong,Z.Liu,J.Montclare
Key ref: Z.Liu et al. (2009). Structural and functional studies of Aspergillus oryzae cutinase: enhanced thermostability and hydrolytic activity of synthetic ester and polyester degradation. J Am Chem Soc, 131, 15711-15716. PubMed id: 19810726
Date:
20-Feb-09     Release date:   06-Oct-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P52956  (CUTI1_ASPOR) -  Cutinase 1
Seq:
Struc:
213 a.a.
187 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.1.1.74  - Cutinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Cutin + H2O = cutin monomers
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biological process     metabolic process   2 terms 
  Biochemical function     carboxylic ester hydrolase activity     3 terms  

 

 
J Am Chem Soc 131:15711-15716 (2009)
PubMed id: 19810726  
 
 
Structural and functional studies of Aspergillus oryzae cutinase: enhanced thermostability and hydrolytic activity of synthetic ester and polyester degradation.
Z.Liu, Y.Gosser, P.J.Baker, Y.Ravee, Z.Lu, G.Alemu, H.Li, G.L.Butterfoss, X.P.Kong, R.Gross, J.K.Montclare.
 
  ABSTRACT  
 
Cutinases are responsible for hydrolysis of the protective cutin lipid polyester matrix in plants and thus have been exploited for hydrolysis of small molecule esters and polyesters. Here we explore the reactivity, stability, and structure of Aspergillus oryzae cutinase and compare it to the well-studied enzyme from Fusarium solani. Two critical differences are highlighted in the crystallographic analysis of the A. oryzae structure: (i) an additional disulfide bond and (ii) a topologically favored catalytic triad with a continuous and deep groove. These structural features of A. oryzae cutinase are proposed to result in an improved hydrolytic activity and altered substrate specificity profile, enhanced thermostability, and remarkable reactivity toward the degradation of the synthetic polyester polycaprolactone. The results presented here provide insight into engineering new cutinase-inspired biocatalysts with tailor-made properties.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21333648 M.Lazniewski, K.Steczkiewicz, L.Knizewski, I.Wawer, and K.Ginalski (2011).
Novel transmembrane lipases of alpha/beta hydrolase fold.
  FEBS Lett, 585, 870-874.  
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