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2K2Q

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

2K2Q の概要
エントリーDOI10.2210/pdb2k2q/pdb
関連するPDBエントリー2GDX 2ron
分子名称Tyrocidine synthetase 3 (Tyrocidine synthetase III), Surfactin synthetase thioesterase subunit (2 entities in total)
機能のキーワード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
由来する生物種Brevibacillus parabrevis
詳細
細胞内の位置Cytoplasm: Q08788
タンパク質・核酸の鎖数2
化学式量合計36557.85
構造登録者
主引用文献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: 18704089
DOI: 10.1038/nature07161
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2k2q
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-04-02に公開中

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