1OAS

O-ACETYLSERINE SULFHYDRYLASE FROM SALMONELLA TYPHIMURIUM


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.200 
  • R-Value Work: 0.172 

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This is version 1.3 of the entry. See complete history


Literature

Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium.

Burkhard, P.Rao, G.S.Hohenester, E.Schnackerz, K.D.Cook, P.F.Jansonius, J.N.

(1998) J Mol Biol 283: 121-133

  • DOI: https://doi.org/10.1006/jmbi.1998.2037
  • Primary Citation of Related Structures:  
    1OAS

  • PubMed Abstract: 

    The last step in cysteine biosynthesis in enteric bacteria is catalyzed by the pyridoxal 5'-phosphate-dependent enzyme O-acetylserine sulfhydrylase. Here we report the crystal structure at 2.2 A resolution of the A-isozyme of O-acetylserine sulfhydrylase isolated from Salmonella typhimurium. O-acetylserine sulfhydrylase shares the same fold with tryptophan synthase-beta from Salmonella typhimurium but the sequence identity level is below 20%. There are some major structural differences: the loops providing the interface to the alpha-subunit in tryptophan synthase-beta and two surface helices of tryptophan synthase-beta are missing in O-acetylserine sulfhydrylase. The hydrophobic channel for indole transport from the alpha to the beta active site of tryptophan synthase-beta is, not unexpectedly, also absent in O-acetylserine sulfhydrylase. The dimer interface, on the other hand, is more or less conserved in the two enzymes. The active site cleft of O-acetylserine sulfhydrylase is wider and therefore more exposed to the solvent. A possible binding site for the substrate O-acetylserine is discussed.


  • Organizational Affiliation

    Department of Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse70, Basel, CH-4056, Switzerland.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
O-ACETYLSERINE SULFHYDRYLASE
A, B
322Salmonella enterica subsp. enterica serovar TyphimuriumMutation(s): 0 
EC: 4.2.99.8
UniProt
Find proteins for P0A1E3 (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720))
Explore P0A1E3 
Go to UniProtKB:  P0A1E3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0A1E3
Sequence Annotations
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  • Reference Sequence
Small Molecules
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.200 
  • R-Value Work: 0.172 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 54.6α = 90
b = 98.2β = 90
c = 145.4γ = 90
Software Package:
Software NamePurpose
MLPHAREphasing
CNSrefinement
MOSFLMdata reduction
CCP4data scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-01-28
    Type: Initial release
  • Version 1.1: 2007-10-16
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2023-12-27
    Changes: Data collection, Database references, Derived calculations