1PC9

Crystal Structure of BnSP-6, a Lys49-Phospholipase A2

1PC9 の概要

• エントリーDOI: 10.2210/pdb1pc9/pdb
• 関連するPDBエントリー: 1PA0
• 分子名称: BnSP-6 (2 entities in total)
• 機能のキーワード: lys49-phospholipase a2, myotoxin, bothrops, venom., hydrolase
• 由来する生物種: Bothrops neuwiedi pauloensis
• 細胞内の位置: Secreted: Q9IAT9
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27362.02

構造登録者

Magro, A.J.,Soares, A.M.,Giglio, J.R.,Fontes, M.R.M. (登録日: 2003-05-16, 公開日: 2004-06-01, 最終更新日: 2024-11-06)

主引用文献

Magro, A.J.,Soares, A.M.,Giglio, J.R.,Fontes, M.R.M.
Crystal structures of BnSP-7 and BnSP-6, two Lys49-phospholipases A(2): quaternary structure and inhibition mechanism insights.
Biochem.Biophys.Res.Commun., 311:713-720, 2003

PubMed Abstract: Phospholipases A(2) are components of Bothrops venoms responsible for disruption of cell membrane integrity via hydrolysis of its phospholipids. A class of PLA(2)-like proteins has been described which despite PLA(2) activity on artificial substrate, due to a D49K mutation, is still highly myonecrotic. This work reports the X-ray structure determination of two Lys49-PLA(2)s from Bothrops neuwiedi pauloensis (BnSP-7 and BnSP-6) and, for the first time, the comparison of eight dimeric Lys49-PLA(2)s. This comparison reveals that there are not just two ("open" and "closed") but at least six different conformations. The binding of fatty acid observed in three recent Lys49-PLA(2) structures seems to be independent of their quaternary conformation. Cys29 polarization by Lys122 is not significant for BnSP-7 and BnSP-6 or other structures not bound by fatty acids. These structures may be in an "active" state when nothing is bound to them and the Lys122/Cys29 interactions are weak or absent.

PubMed: 14623331
DOI: 10.1016/j.bbrc.2003.10.047

実験手法

X-RAY DIFFRACTION (2.5 Å)