5K3W

Structural characterisation of fold IV-transaminase, CpuTA1, from Curtobacterium pusillum


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.218 
  • R-Value Work: 0.163 
  • R-Value Observed: 0.166 

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This is version 1.2 of the entry. See complete history


Literature

Discovery and structural characterisation of new fold type IV-transaminases exemplify the diversity of this enzyme fold.

Pavkov-Keller, T.Strohmeier, G.A.Diepold, M.Peeters, W.Smeets, N.Schurmann, M.Gruber, K.Schwab, H.Steiner, K.

(2016) Sci Rep 6: 38183-38183

  • DOI: https://doi.org/10.1038/srep38183
  • Primary Citation of Related Structures:  
    5K3W

  • PubMed Abstract: 

    Transaminases are useful biocatalysts for the production of amino acids and chiral amines as intermediates for a broad range of drugs and fine chemicals. Here, we describe the discovery and characterisation of new transaminases from microorganisms which were enriched in selective media containing (R)-amines as sole nitrogen source. While most of the candidate proteins were clearly assigned to known subgroups of the fold IV family of PLP-dependent enzymes by sequence analysis and characterisation of their substrate specificity, some of them did not fit to any of these groups. The structure of one of these enzymes from Curtobacterium pusillum, which can convert d-amino acids and various (R)-amines with high enantioselectivity, was solved at a resolution of 2.4 Å. It shows significant differences especially in the active site compared to other transaminases of the fold IV family and thus indicates the existence of a new subgroup within this family. Although the discovered transaminases were not able to convert ketones in a reasonable time frame, overall, the enrichment-based approach was successful, as we identified two amine transaminases, which convert (R)-amines with high enantioselectivity, and can be used for a kinetic resolution of 1-phenylethylamine and analogues to obtain the (S)-amines with e.e.s >99%.


  • Organizational Affiliation

    acib, Austrian Centre of Industrial Biotechnology GmbH, 8010 Graz, Austria.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CpuTA1
A, B
313Curtobacterium pusillumMutation(s): 0 
UniProt
Find proteins for A0A1S4NYF0 (Curtobacterium pusillum)
Explore A0A1S4NYF0 
Go to UniProtKB:  A0A1S4NYF0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A1S4NYF0
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.218 
  • R-Value Work: 0.163 
  • R-Value Observed: 0.166 
  • Space Group: P 62
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 154.428α = 90
b = 154.428β = 90
c = 71.005γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
XDSdata scaling
PHASERphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Austrian Science FundAustriaP24135-N17
FFGAustria--

Revision History  (Full details and data files)

  • Version 1.0: 2016-12-14
    Type: Initial release
  • Version 1.1: 2017-09-06
    Changes: Author supporting evidence
  • Version 1.2: 2024-01-10
    Changes: Data collection, Database references, Refinement description