Structural analysis of membrane-deforming SYLF domain proteins

• Project/Area Number: 15K06985
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Structural biochemistry
• Research Institution: High Energy Accelerator Research Organization
• Principal Investigator: KAWASAKI Masato 大学共同利用機関法人高エネルギー加速器研究機構, 物質構造科学研究所, 准教授 (00342600)
• Co-Investigator(Renkei-kenkyūsha): ITOH Toshiki 神戸大学, バイオシグナル研究センター, 教授 (30313092)
• Project Period (FY): 2015-04-01 – 2018-03-31
• Project Status: Completed (Fiscal Year 2017)
• Budget Amount: ¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000); Fiscal Year 2017: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000); Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000); Fiscal Year 2015: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
• Keywords: X線結晶構造解析 / エンドサイトーシス / 膜変形タンパク質

Outline of Final Research Achievements

SYLF domain is a new member of membrane-deforming protein implicated in endocytosis. The crystal structure of SYLF domain of thermophilic bacteria Thermotoga maritima was determined at 2.2 angstrom resolution Based on the structure, a predicted loop region of human SYLF domain was deleted. The modified human SYLF domain could be crystallized and structure was determined at 2.0 angstrom resolution. SYLF domain adopts a novel fold and the basic surface patches were expected to interact with membrane.