2OKH

Crystal structure of dimeric form of PfFabZ in crystal form3


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.293 
  • R-Value Work: 0.243 
  • R-Value Observed: 0.243 

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This is version 1.3 of the entry. See complete history


Literature

Packing and loop-structure variations in non-isomorphous crystals of FabZ from Plasmodium falciparum

Swarnamukhi, P.L.Sharma, S.K.Padala, P.Surolia, N.Surolia, A.Suguna, K.

(2007) Acta Crystallogr D Biol Crystallogr 63: 458-464

  • DOI: https://doi.org/10.1107/S0907444907003228
  • Primary Citation of Related Structures:  
    2OKH, 2OKI

  • PubMed Abstract: 

    The crystals obtained from various batches of crystallization trials of FabZ from Plasmodium falciparum exhibited non-isomorphism. The c axis of the I222 cell showed a large variation of about 16 A, from c = 81 A to c = 97 A. Complete data sets were collected for three crystal forms with varying lengths of the c axis (form 1, c = 97 A; form 2, c = 92 A; form 3, c = 81 A). The crystal structure of form 1 has been reported previously. Here, the crystal structures of the other two crystal forms are reported and a detailed structural comparison is made of the three crystal forms in order to explore the possible reasons for the existence of non-isomorphism. The conformations of three loops vary between the three crystal forms. The disposition of the loops affects the crystal packing and hence the unit-cell parameter. The crystallization condition and crystallization method employed, which change the evaporation rate, determine the crystal form of the enzyme. The present analysis shows that pH-induced intrinsic conformational changes in the protein play a key role in the observed differences.


  • Organizational Affiliation

    Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-hydroxyacyl-ACP dehydratase
A, B
136Plasmodium falciparumMutation(s): 0 
Gene Names: fabZ
EC: 4.2.1
UniProt
Find proteins for Q965D7 (Plasmodium falciparum)
Explore Q965D7 
Go to UniProtKB:  Q965D7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ965D7
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.293 
  • R-Value Work: 0.243 
  • R-Value Observed: 0.243 
  • Space Group: I 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 69.967α = 90
b = 81.511β = 90
c = 80.8γ = 90
Software Package:
Software NamePurpose
CNSrefinement
HKL-2000data collection
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-04-10
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-10-25
    Changes: Data collection, Database references, Refinement description