2WDO

Crystal structure of the S. coelicolor AcpS in complex with acetyl- CoA at 1.5 A

2WDO の概要

• エントリーDOI: 10.2210/pdb2wdo/pdb
• 関連するPDBエントリー: 2JBZ 2JCA 2WDS 2WDY
• 分子名称: HOLO-[ACYL-CARRIER-PROTEIN] SYNTHASE, MAGNESIUM ION, ACETYL COENZYME *A, ... (7 entities in total)
• 機能のキーワード: phosphopantetheine arm, fatty acid biosynthesis, lipid synthesis, transferase, polyketides
• 由来する生物種: STREPTOMYCES COELICOLOR
• 細胞内の位置: Cytoplasm (By similarity): O86785
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16541.34

構造登録者

Dall'Aglio, P.,Arthur, C.,Crump, M.P.,Crosby, J.,Hadfield, A.T. (登録日: 2009-03-25, 公開日: 2010-04-21, 最終更新日: 2023-12-13)

主引用文献

Dall'Aglio, P.,Arthur, C.,Williams, C.,Vasilakis, K.,Maple, H.J.,Crosby, J.,Crump, M.P.,Hadfield, A.T.
Analysis of Streptomyces Coelicolor Phosphopantetheinyl Transferase, Acps, Reveals the Basis for Relaxed Substrate Specificity.
Biochemistry, 50:5704-, 2011

PubMed Abstract: The transfer of the phosphopantetheine chain from coenzyme A (CoA) to the acyl carrier protein (ACP), a key protein in both fatty acid and polyketide synthesis, is catalyzed by ACP synthase (AcpS). Streptomyces coelicolor AcpS is a doubly promiscuous enzyme capable of activation of ACPs from both fatty acid and polyketide synthesis and catalyzes the transfer of modified CoA substrates. Five crystal structures have been determined, including those of ligand-free AcpS, complexes with CoA and acetyl-CoA, and two of the active site mutants, His110Ala and Asp111Ala. All five structures are trimeric and provide further insight into the mechanism of catalysis, revealing the first detailed structure of a group I active site with the essential magnesium in place. Modeling of ACP binding supported by mutational analysis suggests an explanation for the promiscuity in terms of both ACP partner and modified CoA substrates.

PubMed: 21595442
DOI: 10.1021/BI2003668

実験手法

X-RAY DIFFRACTION (1.56 Å)