2K2Q

complex structure of the external thioesterase of the Surfactin-synthetase with a carrier domain


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 18 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Structural basis for the selectivity of the external thioesterase of the surfactin synthetase.

Koglin, A.Lohr, F.Bernhard, F.Rogov, V.V.Frueh, D.P.Strieter, E.R.Mofid, M.R.Guntert, P.Wagner, G.Walsh, C.T.Marahiel, M.A.Dotsch, V.

(2008) Nature 454: 907-911

  • DOI: https://doi.org/10.1038/nature07161
  • Primary Citation of Related Structures:  
    2K2Q, 2RON

  • PubMed Abstract: 

    Non-ribosomal peptide synthetases (NRPS) and polyketide synthases (PKS) found in bacteria, fungi and plants use two different types of thioesterases for the production of highly active biological compounds. Type I thioesterases (TEI) catalyse the release step from the assembly line of the final product where it is transported from one reaction centre to the next as a thioester linked to a 4'-phosphopantetheine (4'-PP) cofactor that is covalently attached to thiolation (T) domains. The second enzyme involved in the synthesis of these secondary metabolites, the type II thioesterase (TEII), is a crucial repair enzyme for the regeneration of functional 4'-PP cofactors of holo-T domains of NRPS and PKS systems. Mispriming of 4'-PP cofactors by acetyl- and short-chain acyl-residues interrupts the biosynthetic system. This repair reaction is very important, because roughly 80% of CoA, the precursor of the 4'-PP cofactor, is acetylated in bacteria. Here we report the three-dimensional structure of a type II thioesterase from Bacillus subtilis free and in complex with a T domain. Comparison with structures of TEI enzymes shows the basis for substrate selectivity and the different modes of interaction of TEII and TEI enzymes with T domains. Furthermore, we show that the TEII enzyme exists in several conformations of which only one is selected on interaction with its native substrate, a modified holo-T domain.


  • Organizational Affiliation

    Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance and Cluster of Excellence Macromolecular Complexes (CEF), J.W.-Goethe University, 60438 Frankfurt am Main, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Tyrocidine synthetase 3 (Tyrocidine synthetase III)82Brevibacillus parabrevisMutation(s): 0 
Gene Names: tycC
UniProt
Find proteins for O30409 (Brevibacillus parabrevis)
Explore O30409 
Go to UniProtKB:  O30409
Entity Groups  
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UniProt GroupO30409
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Surfactin synthetase thioesterase subunit242Bacillus subtilisMutation(s): 0 
Gene Names: srfADsrfA4
EC: 3.1.2
UniProt
Find proteins for Q08788 (Bacillus subtilis (strain 168))
Explore Q08788 
Go to UniProtKB:  Q08788
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ08788
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 18 

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2008-12-09
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2016-10-19
    Changes: Structure summary
  • Version 1.3: 2018-01-24
    Changes: Structure summary
  • Version 1.4: 2024-05-01
    Changes: Data collection, Database references