2XQZ

Neutron structure of the perdeuterated Toho-1 R274N R276N double mutant beta-lactamase


Experimental Data Snapshot

  • Method: NEUTRON DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.259 
  • R-Value Work: 0.225 
  • R-Value Observed: 0.228 

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This is version 2.1 of the entry. See complete history


Literature

The Active Site Protonation States of Perdeuterated Toho-1 Beta-Lactamase Determined by Neutron Diffraction Support a Role for Glu166 as the General Base in Acylation.

Tomanicek, S.J.Wang, K.K.Weiss, K.L.Blakeley, M.P.Cooper, J.Chen, Y.Coates, L.

(2011) FEBS Lett 585: 364

  • DOI: https://doi.org/10.1016/j.febslet.2010.12.017
  • Primary Citation of Related Structures:  
    2XQZ, 2XR0

  • PubMed Abstract: 

    Room temperature neutron diffraction data of the fully perdeuterated Toho-1 R274N/R276N double mutant β-lactamase in the apo form were used to visualize deuterium atoms within the active site of the enzyme. This perdeuterated neutron structure of the Toho-1 R274N/R276N reveals the clearest picture yet of the ground-state active site protonation states and the complete hydrogen-bonding network in a β-lactamase enzyme. The ground-state active site protonation states detailed in this neutron diffraction study are consistent with previous high-resolution X-ray studies that support the role of Glu166 as the general base during the acylation reaction in the class A β-lactamase reaction pathway.


  • Organizational Affiliation

    Oak Ridge National Laboratory, Neutron Scattering Science Division, Oak Ridge, TN 37831, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
BETA-LACTAMSE TOHO-1260Escherichia coliMutation(s): 2 
EC: 3.5.2.6
UniProt
Find proteins for Q47066 (Escherichia coli)
Explore Q47066 
Go to UniProtKB:  Q47066
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ47066
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: NEUTRON DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.259 
  • R-Value Work: 0.225 
  • R-Value Observed: 0.228 
  • Space Group: P 32 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 72.956α = 90
b = 72.956β = 90
c = 98.526γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
LAUEGENdata reduction
LAUEGENdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-12-22
    Type: Initial release
  • Version 2.0: 2017-12-27
    Changes: Advisory, Atomic model, Derived calculations, Other
  • Version 2.1: 2018-01-31
    Changes: Data collection