4AIW

GAPR-1 with bound inositol hexakisphosphate

4AIW の概要

• エントリーDOI: 10.2210/pdb4aiw/pdb
• 関連するPDBエントリー: 1SMB
• 分子名称: GOLGI-ASSOCIATED PLANT PATHOGENESIS-RELATED PROTEIN 1, INOSITOL HEXAKISPHOSPHATE (3 entities in total)
• 機能のキーワード: lipid-binding protein, golgi apparatus, myristate, lipid binding protein
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17952.35

構造登録者

Schouten, A.,Gros, P.,Helms, J.B. (登録日: 2012-02-15, 公開日: 2012-08-08, 最終更新日: 2023-12-20)

主引用文献

Van Galen, J.,Olrichs, N.K.,Schouten, A.,Serrano, R.L.,Nolte-'T Hoen, E.N.M.,Eerland, R.,Kaloyanova, D.,Gros, P.,Helms, J.B.
Interaction of Gapr-1 with Lipid Bilayers is Regulated by Alternative Homodimerization.
Biochim.Biophys.Acta, 1818:2175-, 2012

PubMed Abstract: Golgi-Associated Plant Pathogenesis-Related protein 1 (GAPR-1) is a mammalian protein that belongs to the superfamily of plant pathogenesis related proteins group 1 (PR-1). GAPR-1 is a peripheral membrane-binding protein that strongly associates with lipid-enriched microdomains at the cytosolic leaflet of Golgi membranes. Little is known about the mechanism of GAPR-1 interaction with membranes. We previously suggested that dimerization plays a role in the function of GAPR-1 and here we report that phytic acid (inositol hexakisphosphate) induces dimerization of GAPR-1 in solution. Elucidation of the crystal structure of GAPR-1 in the presence of phytic acid revealed that the GAPR-1 dimer differs from the previously published GAPR-1 dimer structure. In this structure, one of the monomeric subunits of the crystallographic dimer is rotated by 28.5°. To study the GAPR-1 dimerization properties, we investigated the interaction with liposomes in a light scattering assay and by flow cytometry. In the presence of negatively charged lipids, GAPR-1 caused a rapid and stable tethering of liposomes. [D81K]GAPR-1, a mutant predicted to stabilize the IP6-induced dimer conformation, also caused tethering of liposomes. [A68K]GAPR-1 however, a mutant predicted to stabilize the non-rotated dimer conformation, is capable of binding to liposomes but did not cause liposome tethering. Our combined data suggest that the charge properties of the lipid bilayer can regulate GAPR-1 dynamics as a potential mechanism to modulate GAPR-1 function.

PubMed: 22560898
DOI: 10.1016/J.BBAMEM.2012.04.016

実験手法

X-RAY DIFFRACTION (1.5 Å)