3PLT

Crystal structure of Lsp1 from Saccharomyces cerevisiae

3PLT の概要

• エントリーDOI: 10.2210/pdb3plt/pdb
• 分子名称: Sphingolipid long chain base-responsive protein LSP1 (2 entities in total)
• 機能のキーワード: eisosomes, lsp1, pil1, bar domain, plasma membrane, self-assembly, phosphoprotein, structural protein
• 由来する生物種: Saccharomyces cerevisiae (yeast)
• 細胞内の位置: Cytoplasm, cell cortex: Q12230
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 78244.08

構造登録者

Ziolkowska, N.E.,Walther, T.C. (登録日: 2010-11-15, 公開日: 2011-06-22, 最終更新日: 2024-02-21)

主引用文献

Ziolkowska, N.E.,Karotki, L.,Rehman, M.,Huiskonen, J.T.,Walther, T.C.
Eisosome-driven plasma membrane organization is mediated by BAR domains.
Nat.Struct.Mol.Biol., 18:854-856, 2011

PubMed Abstract: Plasma membranes are organized into domains of different protein and lipid composition. Eisosomes are key complexes for yeast plasma membrane organization, containing primarily Pil1 and Lsp1. Here we show that both proteins consist mostly of a banana-shaped BAR domain common to membrane sculpting proteins, most similar to the ones of amphiphysin, arfaptin 2 and endophilin 2. Our data reveal a previously unrecognized family of BAR-domain proteins involved in plasma membrane organization.

PubMed: 21685922
DOI: 10.1038/nsmb.2080

実験手法

X-RAY DIFFRACTION (2.9 Å)