4AV9

Kluyveromyces lactis Hsv2

4AV9 の概要

• エントリーDOI: 10.2210/pdb4av9/pdb
• 関連するPDBエントリー: 4AV8
• 分子名称: SVP1-LIKE PROTEIN 2, SULFATE ION (3 entities in total)
• 機能のキーワード: lipid binding protein
• 由来する生物種: KLUYVEROMYCES LACTIS
• 細胞内の位置: Vacuole membrane; Peripheral membrane protein (By similarity): Q6CN23
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39508.13

構造登録者

Krick, R.,Busse, R.A.,Scacioc, A.,Stephan, M.,Janshoff, A.,Thumm, M.,Kuhnel, K. (登録日: 2012-05-24, 公開日: 2012-06-13, 最終更新日: 2024-05-08)

主引用文献

Krick, R.,Busse, R.A.,Scacioc, A.,Stephan, M.,Janshoff, A.,Thumm, M.,Kuhnel, K.
Structural and Functional Characterization of the Two Phosphoinositide Binding Sites of Proppins, a Beta-Propeller Protein Family.
Proc.Natl.Acad.Sci.USA, 109:E2042-, 2012

PubMed Abstract: β-propellers that bind polyphosphoinositides (PROPPINs), a eukaryotic WD-40 motif-containing protein family, bind via their predicted β-propeller fold the polyphosphoinositides PtdIns3P and PtdIns(3,5)P(2) using a conserved FRRG motif. PROPPINs play a key role in macroautophagy in addition to other functions. We present the 3.0-Å crystal structure of Kluyveromyces lactis Hsv2, which shares significant sequence homologies with its three Saccharomyces cerevisiae homologs Atg18, Atg21, and Hsv2. It adopts a seven-bladed β-propeller fold with a rare nonvelcro propeller closure. Remarkably, in the crystal structure, the two arginines of the FRRG motif are part of two distinct basic pockets formed by a set of highly conserved residues. In comprehensive in vivo and in vitro studies of ScAtg18 and ScHsv2, we define within the two pockets a set of conserved residues essential for normal membrane association, phosphoinositide binding, and biological activities. Our experiments show that PROPPINs contain two individual phosphoinositide binding sites. Based on docking studies, we propose a model for phosphoinositide binding of PROPPINs.

PubMed: 22753491
DOI: 10.1073/PNAS.1205128109

実験手法

X-RAY DIFFRACTION (3.001 Å)