1HYI

SOLUTION STRUCTURE OF THE EEA1 FYVE DOMAIN COMPLEXED WITH INOSITOL 1,3-BISPHOSPHATE

1HYI の概要

• エントリーDOI: 10.2210/pdb1hyi/pdb
• 関連するPDBエントリー: 1HYJ
• NMR情報: BMRB: 4579
• 分子名称: ENDOSOME-ASSOCIATED PROTEIN, ZINC ION, PHOSPHORIC ACID MONO-(2,3,4,6-TETRAHYDROXY-5-PHOSPHONOOXY-CYCLOHEXYL) ESTER (3 entities in total)
• 機能のキーワード: beta sheet, alpha helix, zinc cluster, ptdins(3)p, endocytosis-exocytosis complex, endocytosis/exocytosis
• 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: 7703.23

構造登録者

Kutateladze, T.,Overduin, M. (登録日: 2001-01-19, 公開日: 2001-03-14, 最終更新日: 2024-05-22)

主引用文献

Kutateladze, T.,Overduin, M.
Structural mechanism of endosome docking by the FYVE domain.
Science, 291:1793-1796, 2001

PubMed Abstract: The recruitment of trafficking and signaling proteins to membranes containing phosphatidylinositol 3-phosphate [PtdIns(3)P] is mediated by FYVE domains. Here, the solution structure of the FYVE domain of the early endosome antigen 1 protein (EEA1) in the free state was compared with the structures of the domain complexed with PtdIns(3)P and mixed micelles. The multistep binding mechanism involved nonspecific insertion of a hydrophobic loop into the lipid bilayer, positioning and activating the binding pocket. Ligation of PtdIns(3)P then induced a global structural change, drawing the protein termini over the bound phosphoinositide by extension of a hinge. Specific recognition of the 3-phosphate was determined indirectly and directly by two clusters of conserved arginines.

PubMed: 11230696
DOI: 10.1126/science.291.5509.1793

実験手法

SOLUTION NMR