2K2Q
complex structure of the external thioesterase of the Surfactin-synthetase with a carrier domain
Summary for 2K2Q
Entry DOI | 10.2210/pdb2k2q/pdb |
Related | 2GDX 2ron |
Descriptor | Tyrocidine synthetase 3 (Tyrocidine synthetase III), Surfactin synthetase thioesterase subunit (2 entities in total) |
Functional Keywords | thioesterase, a/b-hydrolase, nrps, non-ribosomal peptide synthetase, type ii thioesterase, antibiotic biosynthesis, ligase, multifunctional enzyme, phosphopantetheine, sporulation, stress response, ligase-hydrolase complex, ligase/hydrolase |
Biological source | Brevibacillus parabrevis More |
Cellular location | Cytoplasm: Q08788 |
Total number of polymer chains | 2 |
Total formula weight | 36557.85 |
Authors | 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. (deposition date: 2008-04-10, release date: 2008-12-09, Last modification date: 2024-05-01) |
Primary citation | 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. Structural basis for the selectivity of the external thioesterase of the surfactin synthetase. Nature, 454:907-911, 2008 Cited by 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. PubMed: 18704089DOI: 10.1038/nature07161 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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