7X0D

Crystal structure of phospholipase A1, CaPLA1

7X0D の概要

• エントリーDOI: 10.2210/pdb7x0d/pdb
• 分子名称: Phospholipase A1, SULFATE ION (3 entities in total)
• 機能のキーワード: phospholipase a1, hydrolase
• 由来する生物種: Capsicum annuum
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 181454.10

構造登録者

Heo, Y.,Lee, I.,Moon, S.,Lee, W. (登録日: 2022-02-21, 公開日: 2022-04-13, 最終更新日: 2023-11-29)

主引用文献

Heo, Y.,Lee, I.,Moon, S.,Yun, J.H.,Kim, E.Y.,Park, S.Y.,Park, J.H.,Kim, W.T.,Lee, W.
Crystal Structures of the Plant Phospholipase A1 Proteins Reveal a Unique Dimerization Domain.
Molecules, 27:-, 2022

PubMed Abstract: Phospholipase is an enzyme that hydrolyzes various phospholipid substrates at specific ester bonds and plays important roles such as membrane remodeling, as digestive enzymes, and the regulation of cellular mechanism. Phospholipase proteins are divided into following the four major groups according to the ester bonds they cleave off: phospholipase A1 (PLA1), phospholipase A2 (PLA2), phospholipase C (PLC), and phospholipase D (PLD). Among the four phospholipase groups, PLA1 has been less studied than the other phospholipases. Here, we report the first molecular structures of plant PLA1s: AtDSEL and CaPLA1 derived from and , respectively. AtDSEL and CaPLA1 are novel PLA1s in that they form homodimers since PLAs are generally in the form of a monomer. The dimerization domain at the C-terminal of the AtDSEL and CaPLA1 makes hydrophobic interactions between each monomer, respectively. The C-terminal domain is also present in PLA1s of other plants, but not in PLAs of mammals and fungi. An activity assay of AtDSEL toward various lipid substrates demonstrates that AtDSEL is specialized for the cleavage of -1 acyl chains. This report reveals a new domain that exists only in plant PLA1s and suggests that the domain is essential for homodimerization.

PubMed: 35408716
DOI: 10.3390/molecules27072317

実験手法

X-RAY DIFFRACTION (2.3972515576 Å)