1EQP

EXO-B-(1,3)-GLUCANASE FROM CANDIDA ALBICANS


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.195 
  • R-Value Work: 0.156 
  • R-Value Observed: 0.154 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Minor structural consequences of alternative CUG codon usage (Ser for Leu) in Candida albicans exoglucanase.

Cutfield, J.F.Sullivan, P.A.Cutfield, S.M.

(2000) Protein Eng 13: 735-738

  • DOI: https://doi.org/10.1093/protein/13.10.735
  • Primary Citation of Related Structures:  
    1EQP

  • PubMed Abstract: 

    In some species of Candida the CUG codon is encoded as serine and not leucine. In the case of the exo-beta-1,3-glucanase from the pathogenic fungus C. albicans there are two such translational events, one in the prepro-leader sequence and the other at residue 64. Overexpression of active mature enzyme in a yeast host indicated that these two positions are tolerant to substitution. By comparing the crystal structure of the recombinant protein with that of the native (presented here), it is seen how either serine or leucine can be accommodated at position 64. Examination of the relatively few solved protein structures from C. albicans indicates that other CUG encoded serines are also found at non-essential surface sites. However such codon usage is rare in C. albicans, in contrast to C. rugosa, with direct implications for respective recombinant protein production.


  • Organizational Affiliation

    Biochemistry Department, School of Medical Sciences, University of Otago, PO Box 56, Dunedin, New Zealand. john.cutfield@stonebow.otago.ac.nz


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
EXO-B-(1,3)-GLUCANASE394Candida albicansMutation(s): 0 
EC: 3.2.1.58
UniProt
Find proteins for P29717 (Candida albicans (strain SC5314 / ATCC MYA-2876))
Explore P29717 
Go to UniProtKB:  P29717
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP29717
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.195 
  • R-Value Work: 0.156 
  • R-Value Observed: 0.154 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 60.1α = 90
b = 65.3β = 90
c = 96.4γ = 90
Software Package:
Software NamePurpose
ROTAVATAdata reduction
REFMACrefinement
CCP4data scaling
ROTAVATAdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2001-02-28
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-10-04
    Changes: Refinement description