4G09

The crystal structure of the C366S mutant of HDH from Brucella suis in complex with a substituted benzyl ketone


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.253 
  • R-Value Work: 0.213 
  • R-Value Observed: 0.213 

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Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Structural basis for the rational design of new anti-Brucella agents: The crystal structure of the C366S mutant of l-histidinol dehydrogenase from Brucella suis.

D'ambrosio, K.Lopez, M.Dathan, N.A.Ouahrani-Bettache, S.Kohler, S.Ascione, G.Monti, S.M.Winum, J.Y.De Simone, G.

(2014) Biochimie 97: 114-120

  • DOI: https://doi.org/10.1016/j.biochi.2013.09.028
  • Primary Citation of Related Structures:  
    4G07, 4G09

  • PubMed Abstract: 

    L-Histidinol dehydrogenase from Brucella suis (BsHDH) is an enzyme involved in the histidine biosynthesis pathway which is absent in mammals, thus representing a very interesting target for the development of anti-Brucella agents. In this paper we report the crystallographic structure of a mutated form of BsHDH both in its unbound form and in complex with a nanomolar inhibitor. These studies provide the first structural background for the rational design of potent HDH inhibitors, thus offering new hints for clinical applications.


  • Organizational Affiliation

    Istituto di Biostrutture e Bioimmagini-CNR, Via Mezzocannone 16, 80134 Napoli, Italy.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Histidinol dehydrogenase438Brucella suis 1330Mutation(s): 1 
Gene Names: hisDBR0252BS1330_I0253
EC: 1.1.1.23
UniProt
Find proteins for Q8G2R2 (Brucella suis biovar 1 (strain 1330))
Explore Q8G2R2 
Go to UniProtKB:  Q8G2R2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8G2R2
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.253 
  • R-Value Work: 0.213 
  • R-Value Observed: 0.213 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 76.654α = 90
b = 105.072β = 90
c = 111.25γ = 90
Software Package:
Software NamePurpose
CNSrefinement
DENZOdata reduction
HKL-2000data scaling
CNSphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-10-02
    Type: Initial release
  • Version 1.1: 2013-11-06
    Changes: Database references
  • Version 1.2: 2014-02-05
    Changes: Database references
  • Version 1.3: 2024-02-28
    Changes: Data collection, Database references, Derived calculations