Development of new protein cages using domain swapping

2016 Fiscal Year Final Research Report

• Project/Area Number: 15K13744
• Research Category: Grant-in-Aid for Challenging Exploratory Research
• Allocation Type: Multi-year Fund
• Research Field: Bio-related chemistry
• Research Institution: Nara Institute of Science and Technology
• Principal Investigator: HIROTA Shun 奈良先端科学技術大学院大学, 物質創成科学研究科, 教授 (90283457)
• Co-Investigator(Renkei-kenkyūsha): HIGUCHI Yoshiki 兵庫県立大学, 大学院生命理学研究科, 教授 (90183574) ; NAGAO Satoshi 奈良先端科学技術大学院大学, 物質創成科学研究科, 助教 (30452535)
• Project Period (FY): 2015-04-01 – 2017-03-31
• Keywords: タンパク質 / 生体分子 / ナノバイオ / 超分子化学 / タンパク質構造体 / タンパク質ケージ / ドメインスワッピング

Outline of Final Research Achievements

Cytochrome (cyt) cb562 oligomers were constructed, and it was found that the dimer of cyt cb562 forms a domain-swapped structure. Three domain-swapped cyt cb562 dimers formed a unique cage structure with a Zn-SO4 cluster inside the cavity. The Zn-SO4 cluster consisted of fifteen Zn2+ and seven SO42- ions, whereas six additional Zn2+ ions were detected inside the cavity. Fusion proteins comprising the subunits of different homo oligomeric proteins were designed. The two subunits were connected with a 3-helix bundle protein in the fusion proteins. A tetramer and a hexamer were constructed with the fusion proteins, and the structures of the tetramer and hexamer were analyzed by small-angle X-ray scattering and high-speed atomic force microscopy methods.

Free Research Field

タンパク質科学