Structure basis for E2-E3 interation in plant Atg conjugation system

2014 Fiscal Year Final Research Report

• Project/Area Number: 25871076
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Structural biochemistry; Functional biochemistry
• Research Institution: Microbial Chemistry Research Foundation
• Principal Investigator: MATOBA Kazuaki 公益財団法人微生物化学研究会, 微生物化学研究所, 研究員 (60613792)
• Project Period (FY): 2013-04-01 – 2015-03-31
• Keywords: X線結晶構造解析 / オートファジー

Outline of Final Research Achievements

We identified the minimum binding region of Atg3 for Atg12 by in vitro pull-down assay using Arabidopsis thaliana (At) homologs and crystallized the AtAtg12b-AtAtg3 peptide complex. The side-chain of AtAtg3 Asp-Met is bound deeply to the pocket of AtAtg12b. The importance of AtAtg3 Met157 for AtAtg12b binding was confirmed by mutational analysis. These data establish the basis for E2-E3 interaction in the plant Atg system.

Free Research Field

構造生物学