7UK4

KS-AT di-domain of mycobacterial Pks13 with endogenous KS ligand bound

7UK4 の概要

• エントリーDOI: 10.2210/pdb7uk4/pdb
• 関連するPDBエントリー: 8CUY 8CUZ 8CV0 8CV1
• EMDBエントリー: 26574 27002 27003 27004 27005
• 分子名称: Polyketide synthase PKS13, UNKNOWN LIGAND (3 entities in total)
• 機能のキーワード: mycolic acid synthesis, ketosynthase, acyltransferase, multi-domain assembly, biosynthetic protein
• 由来する生物種: Mycolicibacterium smegmatis MC2 155
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 397891.78

構造登録者

Kim, S.K.,Dickinson, M.S.,Finer-Moore, J.S.,Rosenberg, O.S.,Stroud, R.M. (登録日: 2022-03-31, 公開日: 2023-02-15, 最終更新日: 2024-10-23)

主引用文献

Kim, S.K.,Dickinson, M.S.,Finer-Moore, J.,Guan, Z.,Kaake, R.M.,Echeverria, I.,Chen, J.,Pulido, E.H.,Sali, A.,Krogan, N.J.,Rosenberg, O.S.,Stroud, R.M.
Structure and dynamics of the essential endogenous mycobacterial polyketide synthase Pks13.
Nat.Struct.Mol.Biol., 30:296-308, 2023

PubMed Abstract: The mycolic acid layer of the Mycobacterium tuberculosis cell wall is essential for viability and virulence, and the enzymes responsible for its synthesis are targets for antimycobacterial drug development. Polyketide synthase 13 (Pks13) is a module encoding several enzymatic and transport functions that carries out the condensation of two different long-chain fatty acids to produce mycolic acids. We determined structures by cryogenic-electron microscopy of dimeric multi-enzyme Pks13 purified from mycobacteria under normal growth conditions, captured with native substrates. Structures define the ketosynthase (KS), linker and acyl transferase (AT) domains at 1.8 Å resolution and two alternative locations of the N-terminal acyl carrier protein. These structures suggest intermediate states on the pathway for substrate delivery to the KS domain. Other domains, visible at lower resolution, are flexible relative to the KS-AT core. The chemical structures of three bound endogenous long-chain fatty acid substrates were determined by electrospray ionization mass spectrometry.

PubMed: 36782050
DOI: 10.1038/s41594-022-00918-0

実験手法

ELECTRON MICROSCOPY (1.94 Å)