1UZI

C3 EXOENZYME FROM CLOSTRIDIUM BOTULINUM, TETRAGONAL FORM


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.89 Å
  • R-Value Free: 0.253 
  • R-Value Work: 0.205 
  • R-Value Observed: 0.207 

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This is version 1.3 of the entry. See complete history


Literature

C3 Exoenzyme from Clostridium Botulinum: Structure of a Tetragonal Crystal Form and a Reassessment of Nad-Induced Flexure

Evans, H.R.Holloway, D.E.Sutton, J.M.Ayriss, J.Shone, C.C.Acharya, K.R.

(2004) Acta Crystallogr D Biol Crystallogr 60: 1502

  • DOI: https://doi.org/10.1107/S0907444904011680
  • Primary Citation of Related Structures:  
    1UZI

  • PubMed Abstract: 

    C3 exoenzyme from Clostridium botulinum (C3bot1) ADP-ribosylates and thereby inactivates Rho A, B and C GTPases in mammalian cells. The structure of a tetragonal crystal form has been determined by molecular replacement and refined to 1.89 A resolution. It is very similar to the apo structures determined previously from two different monoclinic crystal forms. An objective reassessment of available apo and nucleotide-bound C3bot1 structures indicates that, contrary to a previous report, the protein possesses a rigid core formed largely of beta-strands and that the general flexure that accompanies NAD binding is concentrated in two peripheral lobes. Tetragonal crystals disintegrate in the presence of NAD, most likely because of disruption of essential crystal contacts.


  • Organizational Affiliation

    Department of Biology and Biochemistry, University of Bath, Claverton Down, BA2 7AY, England.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
MONO-ADP-RIBOSYLTRANSFERASE C3
A, B
211Clostridium botulinumMutation(s): 0 
EC: 2.4.2.30
UniProt
Find proteins for P15879 (Clostridium botulinum D phage)
Explore P15879 
Go to UniProtKB:  P15879
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP15879
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.89 Å
  • R-Value Free: 0.253 
  • R-Value Work: 0.205 
  • R-Value Observed: 0.207 
  • Space Group: I 4
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 73.293α = 90
b = 73.293β = 90
c = 218.233γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
HKL-2000data reduction
SCALEPACKdata scaling
MOLREPphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-07-29
    Type: Initial release
  • Version 1.1: 2011-05-07
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-12-13
    Changes: Data collection, Database references, Refinement description