7CNW

Crystal structure of Apo PSD from E. coli (1.90 A)

7CNW の概要

• エントリーDOI: 10.2210/pdb7cnw/pdb
• 分子名称: Phosphatidylserine decarboxylase beta chain, Phosphatidylserine decarboxylase alpha chain, DODECYL-BETA-D-MALTOSIDE, ... (5 entities in total)
• 機能のキーワード: phosphatidylserine decarboxylase, pyruvoyl-dependent decarboxylase, auto-cleaved, serine protease, membrane protein, lyase
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 67832.29

構造登録者

Kim, J.,Cho, G. (登録日: 2020-08-03, 公開日: 2021-03-24, 最終更新日: 2024-11-20)

主引用文献

Cho, G.,Lee, E.,Kim, J.
Structural insights into phosphatidylethanolamine formation in bacterial membrane biogenesis.
Sci Rep, 11:5785-5785, 2021

PubMed Abstract: Phosphatidylethanolamine (PE), a major component of the cellular membrane across all domains of life, is synthesized exclusively by membrane-anchored phosphatidylserine decarboxylase (PSD) in most bacteria. The enzyme undergoes auto-cleavage for activation and utilizes the pyruvoyl moiety to form a Schiff base intermediate with PS to facilitate decarboxylation. However, the structural basis for self-maturation, PS binding, and decarboxylation processes directed by PSD remain unclear. Here, we present X-ray crystal structures of PSD from Escherichia coli, representing an apo form and a PE-bound complex, in which the phospholipid is chemically conjugated to the essential pyruvoyl residue, mimicking the Schiff base intermediate. The high-resolution structures of PE-complexed PSD clearly illustrate extensive hydrophobic interactions with the fatty acyl chains of the phospholipid, providing insights into the broad specificity of the enzyme over a wide range of cellular PS. Furthermore, these structures strongly advocate the unique topology of the enzyme in a lipid bilayer environment, where the enzyme associates with cell membranes in a monotopic fashion via the N-terminal domain composed of three amphipathic helices. Lastly, mutagenesis analyses reveal that E. coli PSD primarily employs D90/D142-H144-S254 to achieve auto-cleavage for the proenzyme maturation, where D90 and D142 act in complementary to each other.

PubMed: 33707636
DOI: 10.1038/s41598-021-85195-5
主引用文献が同じPDBエントリー

実験手法

X-RAY DIFFRACTION (1.9 Å)