4NA3

Crystal Structure of the second ketosynthase from the bacillaene polyketide synthase bound to a hexanoyl substrate mimic

4NA3 の概要

• エントリーDOI: 10.2210/pdb4na3/pdb
• 関連するPDBエントリー: 2HG4 2QO3 4NA1 4NA2
• 分子名称: Polyketide synthase PksJ, SULFATE ION (3 entities in total)
• 機能のキーワード: condensing enzyme fold, transferase
• 由来する生物種: Bacillus subtilis subsp. subtilis
• 細胞内の位置: Cytoplasm: P40806
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 141568.55

構造登録者

Gay, D.C.,Gay, G.R.,Keatinge-Clay, A.T. (登録日: 2013-10-21, 公開日: 2014-02-19, 最終更新日: 2023-09-20)

主引用文献

Gay, D.C.,Gay, G.,Axelrod, A.J.,Jenner, M.,Kohlhaas, C.,Kampa, A.,Oldham, N.J.,Piel, J.,Keatinge-Clay, A.T.
A close look at a ketosynthase from a trans-acyltransferase modular polyketide synthase.
Structure, 22:444-451, 2014

PubMed Abstract: The recently discovered trans-acyltransferase modular polyketide synthases catalyze the biosynthesis of a wide range of bioactive natural products in bacteria. Here we report the structure of the second ketosynthase from the bacillaene trans-acyltransferase polyketide synthase. This 1.95 Å resolution structure provides the highest resolution view available of a modular polyketide synthase ketosynthase and reveals a flanking subdomain that is homologous to an ordered linker in cis-acyltransferase modular polyketide synthases. The structure of the cysteine-to-serine mutant of the ketosynthase acylated by its natural substrate provides high-resolution details of how a native polyketide intermediate is bound and helps explain the basis of ketosynthase substrate specificity. The substrate range of the ketosynthase was further investigated by mass spectrometry.

PubMed: 24508341
DOI: 10.1016/j.str.2013.12.016

実験手法

X-RAY DIFFRACTION (2.89 Å)