3RFI

Crystal structure of the saposin-like domain of plant aspartic protease from Solanum tuberosum

3RFI の概要

• エントリーDOI: 10.2210/pdb3rfi/pdb
• 分子名称: Asp (2 entities in total)
• 機能のキーワード: aspartic protease, psi, saposin, hydrolase
• 由来する生物種: Solanum tuberosum (potatoes)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11779.51

構造登録者

Bhaumik, P.,Wlodawer, A. (登録日: 2011-04-06, 公開日: 2011-06-15, 最終更新日: 2024-11-06)

主引用文献

Bryksa, B.C.,Bhaumik, P.,Magracheva, E.,De Moura, D.C.,Kurylowicz, M.,Zdanov, A.,Dutcher, J.R.,Wlodawer, A.,Yada, R.Y.
Structure and Mechanism of the Saposin-like Domain of a Plant Aspartic Protease.
J.Biol.Chem., 286:28265-28275, 2011

PubMed Abstract: Many plant aspartic proteases contain an additional sequence of ~100 amino acids termed the plant-specific insert, which is involved in host defense and vacuolar targeting. Similar to all saposin-like proteins, the plant-specific insert functions via protein-membrane interactions; however, the structural basis for such interactions has not been studied, and the nature of plant-specific insert-mediated membrane disruption has not been characterized. In the present study, the crystal structure of the saposin-like domain of potato aspartic protease was resolved at a resolution of 1.9 Å, revealing an open V-shaped configuration similar to the open structure of human saposin C. Notably, vesicle disruption activity followed Michaelis-Menten-like kinetics, a finding not previously reported for saposin-like proteins including plant-specific inserts. Circular dichroism data suggested that secondary structure was pH-dependent in a fashion similar to influenza A hemagglutinin fusion peptide. Membrane effects characterized by atomic force microscopy and light scattering indicated bilayer solubilization as well as fusogenic activity. Taken together, the present study is the first report to elucidate the membrane interaction mechanism of plant saposin-like domains whereby pH-dependent membrane interactions resulted in bilayer fusogenic activity that probably arose from a viral type pH-dependent helix-kink-helix motif at the plant-specific insert N terminus.

PubMed: 21676875
DOI: 10.1074/jbc.M111.252619

実験手法

X-RAY DIFFRACTION (1.9 Å)