2k2q

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

spinqualitylabelsall models 2k2q, 18 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2k2q is a 2 chain structure with sequence from Bacillus subtilis and Brevibacillus parabrevis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2ron, 2gdx Gene: tycC (Brevibacillus parabrevis), srfAD, srfA4 (Bacillus subtilis) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Warning: this is a large structure, and loading might take a long time or not happen at all. Function [TYCC_BREPA] Incorporates six amino acids (for tyrocidine A, Asn, Gln, Tyr, Val, Orn, and Leu) in their L-configuration into the peptide product. [SRFAD_BACSU] Probable thioesterase involved in the biosynthesis of surfactin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structural basis for the selectivity of the external thioesterase of the surfactin synthetase.,Koglin A, Lohr F, Bernhard F, Rogov VV, Frueh DP, Strieter ER, Mofid MR, Guntert P, Wagner G, Walsh CT, Marahiel MA, Dotsch V Nature. 2008 Aug 14;454(7206):907-11. PMID:18704089 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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