4V38

Apo-structure of alpha2,3-sialyltransferase variant 1 from Pasteurella dagmatis

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.96 Å
  • R-Value Free: 0.244 
  • R-Value Work: 0.190 
  • R-Value Observed: 0.193 

Starting Model: experimental
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This is version 1.2 of the entry. See complete history. 


Literature

Complete Switch from Alpha2,3- to Alpha2,6-Regioselectivity in Pasteurella Dagmatis Beta-D-Galactoside Sialyltransferase by Active-Site Redesign

Schmoelzer, K., Czabany, T., Pavkov-Keller, T., Luley-Goedl, C., Ribitsch, D., Schwab, H., Gruber, K., Nidetzky, B.

(2015) Chem Commun (Camb) 51: 3083

  • DOI: https://doi.org/10.1039/c4cc09772f
  • Primary Citation of Related Structures:  
    4V2U, 4V38, 4V39, 4V3B, 4V3C

  • PubMed Abstract: 

    Structure-guided active-site redesign of a family GT-80 β-D-galactoside sialyltransferase (from Pasteurella dagmatis) to change enzyme regioselectivity from α-2,3 in the wild type to α-2,6 in a P7H-M117A double mutant is reported. Biochemical data for sialylation of lactose together with protein crystal structures demonstrate highly precise enzyme engineering.

    • Organizational Affiliation: 

    Austrian Centre of Industrial Biotechnology, Petersgasse 14, 8010 Graz, Austria.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
SIALYLTRANSFERASE388Pasteurella dagmatisMutation(s): 1 
UniProt
Find proteins for K9UUI6 (Pasteurella dagmatis)
Explore K9UUI6 
Go to UniProtKB:  K9UUI6
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupK9UUI6
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.96 Å
  • R-Value Free: 0.244 
  • R-Value Work: 0.190 
  • R-Value Observed: 0.193 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 112.22α = 90
b = 57.09β = 111.36
c = 80.15γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
XDSdata scaling
PHASERphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-04-08
    Type: Initial release
  • Version 1.1: 2017-09-13
    Changes: Data collection
  • Version 1.2: 2024-01-10
    Changes: Data collection, Database references, Other, Refinement description