2CZQ

A novel cutinase-like protein from Cryptococcus sp.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.05 Å
  • R-Value Free: 0.157 
  • R-Value Work: 0.147 
  • R-Value Observed: 0.148 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Crystal structure and enhanced activity of a cutinase-like enzyme from Cryptococcus sp. strain S-2

Kodama, Y.Masaki, K.Kondo, H.Suzuki, M.Tsuda, S.Nagura, T.Shimba, N.Suzuki, E.Iefuji, H.

(2009) Proteins 77: 710-717

  • DOI: https://doi.org/10.1002/prot.22484
  • Primary Citation of Related Structures:  
    2CZQ

  • PubMed Abstract: 

    The structural and enzymatic characteristics of a cutinase-like enzyme (CLE) from Cryptococcus sp. strain S-2, which exhibits remote homology to a lipolytic enzyme and a cutinase from the fungus Fusarium solani (FS cutinase), were compared to investigate the unique substrate specificity of CLE. The crystal structure of CLE was solved to a 1.05 A resolution. Moreover, hydrolysis assays demonstrated the broad specificity of CLE for short and long-chain substrates, as well as the preferred specificity of FS cutinase for short-chain substrates. In addition, site-directed mutagenesis was performed to increase the hydrolysis activity on long-chain substrates, indicating that the hydrophobic aromatic residues are important for the specificity to the long-chain substrate. These results indicate that hydrophobic residues, especially the aromatic ones exposed to solvent, are important for retaining lipase activity.


  • Organizational Affiliation

    Institute of Life Sciences, Ajinomoto Co., Inc., Kawasaki-ku, Kawasaki-shi 210-8681, Japan.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
cutinase-like protein
A, B
205Cryptococcus sp. S-2Mutation(s): 0 
EC: 3.1.1
Membrane Entity: Yes 
UniProt
Find proteins for Q874E9 (Cryptococcus sp. S-2)
Explore Q874E9 
Go to UniProtKB:  Q874E9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ874E9
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.05 Å
  • R-Value Free: 0.157 
  • R-Value Work: 0.147 
  • R-Value Observed: 0.148 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 34.478α = 90
b = 82.807β = 90
c = 123.514γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
HKL-2000data reduction
CCP4data scaling
SOLVEphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-07-14
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Source and taxonomy, Version format compliance
  • Version 1.3: 2012-06-13
    Changes: Database references