Structural biology of phage long tail fiber protein and host recognition

2016 Fiscal Year Final Research Report

• Project/Area Number: 25440066
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Biophysics
• Research Institution: Tokyo Institute of Technology
• Principal Investigator: Kanamaru Shuji 東京工業大学, 生命理工学院, 助教 (50376951)
• Project Period (FY): 2013-04-01 – 2017-03-31
• Keywords: バクテリオファージ / ウイルス / 構造蛋白質 / 繊維状蛋白質 / X線結晶構造解析 / 宿主認識

Outline of Final Research Achievements

We over-expressed, purified and crystallized a C-terminal 564 residues of gp34, proximal long tail fiber, of bacteriophage T4. A determined crystal structure of gp34C774-1289 is trimeric fibrous protein which is 18nm long. In detail, there are three-stranded beta-helix and beta-prism domains which are found in other phage tail protein. Thus we conclude that the phage tail proteins are evolved with utilizing the “tail parts domains” to obtain their ability for their infection.
We also purified gp38 as a complex with C-terminal portion of gp37 by co-expression system.

Free Research Field

構造生物学