1OCS

Crystal structure of the yeast PX-doamin protein Grd19p (sorting nexin3) complexed to phosphatidylinosytol-3-phosphate.

1OCS の概要

• エントリーDOI: 10.2210/pdb1ocs/pdb
• 関連するPDBエントリー: 1OCU
• 分子名称: SORTING NEXIN GRD19, GLYCEROL (3 entities in total)
• 機能のキーワード: sorting protein, sorting nexin, px-domain, yeast protein
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• 細胞内の位置: Cytoplasm: Q08826
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18968.91

構造登録者

Zhou, C.Z.,Li De La Sierra-Gallay, I.,Cheruel, S.,Collinet, B.,Minard, P.,Blondeau, K.,Henkes, G.,Aufrere, R.,Leulliot, N.,Graille, M.,Sorel, I.,Savarin, P.,De La Torre, F.,Poupon, A.,Janin, J.,Van Tilbeurgh, H. (登録日: 2003-02-10, 公開日: 2003-12-12, 最終更新日: 2024-10-16)

主引用文献

Zhou, C.Z.,Li De La Sierra-Gallay, I.,Cheruel, S.,Collinet, B.,Minard, P.,Blondeau, K.,Henkes, G.,Aufrere, R.,Leulliot, N.,Graille, M.,Sorel, I.,Savarin, P.,De La Torre, F.,Poupon, A.,Janin, J.,Van Tilbeurgh, H.
Crystal Structure of the Yeast Phox Homology (Px) Protein Grd19P (Sorting Nexin 3) Complexed to Phosphatidylinositol-3-Phosphate
J.Biol.Chem., 278:50371-, 2003

PubMed Abstract: Phox homology (PX) domains have been recently identified in a number of different proteins and are involved in various cellular functions such as vacuolar targeting and membrane protein trafficking. It was shown that these modules of about 130 amino acids specifically binding to phosphoinositides and that this interaction is crucial for their cellular function. The yeast genome contains 17 PX domain proteins. One of these, Grd19p, is involved in the localization of the late Golgi membrane proteins DPAP A and Kex2p. Grd19p consists of the PX domain with 30 extra residues at the N-terminal and is homologous to the functionally characterized human sorting nexin protein SNX3. We determined the 2.0 A crystal structure of Grd19p in the free form and in complex with d-myo-phosphatidylinositol 3-phosphate (diC4PtdIns(3)P), representing the first case of both free and ligand-bound conformations of the same PX module. The ligand occupies a well defined positively charged binding pocket at the interface between the beta-sheet and alpha-helical parts of the molecule. The structure of the free and bound protein are globally similar but show some significant differences in a region containing a polyproline peptide and a putative membrane attachment site.

PubMed: 14514667
DOI: 10.1074/JBC.M304392200

実験手法

X-RAY DIFFRACTION (2.03 Å)