1NM2

Malonyl-CoA:ACP Transacylase

1NM2 の概要

• エントリーDOI: 10.2210/pdb1nm2/pdb
• 分子名称: malonyl CoA:acyl carrier protein malonyltransferase, NICKEL (II) ION, ACETIC ACID, ... (4 entities in total)
• 機能のキーワード: alpha/beta hydrolase-like core, acetate bound to active site mimicking a malonyl group, transferase
• 由来する生物種: Streptomyces coelicolor
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32425.51

構造登録者

Keatinge-Clay, A.T.,Shelat, A.A.,Savage, D.F.,Tsai, S.,Miercke, L.J.W.,O'Connell III, J.D.,Khosla, C.,Stroud, R.M. (登録日: 2003-01-08, 公開日: 2003-01-21, 最終更新日: 2023-08-16)

主引用文献

Keatinge-Clay, A.T.,Shelat, A.A.,Savage, D.F.,Tsai, S.,Miercke, L.J.W.,O'Connell III, J.D.,Khosla, C.,Stroud, R.M.
Catalysis, Specificity, and ACP Docking Site of Streptomyces coelicolor Malonyl-CoA:ACP Transacylase
Structure, 11:147-154, 2003

PubMed Abstract: Malonyl-CoA:ACP transacylase (MAT), the fabD gene product of Streptomyces coelicolor A3(2), participates in both fatty acid and polyketide synthesis pathways, transferring malonyl groups that are used as extender units in chain growth from malonyl-CoA to pathway-specific acyl carrier proteins (ACPs). Here, the 2.0 A structure reveals an invariant arginine bound to an acetate that mimics the malonyl carboxylate and helps define the extender unit binding site. Catalysis may only occur when the oxyanion hole is formed through substrate binding, preventing hydrolysis of the acyl-enzyme intermediate. Macromolecular docking simulations with actinorhodin ACP suggest that the majority of the ACP docking surface is formed by a helical flap. These results should help to engineer polyketide synthases (PKSs) that produce novel polyketides.

PubMed: 12575934
DOI: 10.1016/S0969-2126(03)00004-2

実験手法

X-RAY DIFFRACTION (2 Å)