2016 Fiscal Year Final Research Report
Structural and functional analysis of acyltransferase that possesses a unique substrate specificity
| Project/Area Number |
15K18679
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Applied biochemistry
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| Research Institution | Tokyo Institute of Technology |
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Principal Investigator |
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| Project Period (FY) |
2015-04-01 – 2017-03-31
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| Keywords | 微生物酵素 / 結晶構造解析 / ポリケタイド合成酵素 / アシル基転移酵素 / タンパク質間相互作用 / クロスリンク |
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| Outline of Final Research Achievements |
Acyltransferases are key determinants of building block specificity in polyketide biosynthesis. Despite the importance of protein-protein interactions between acyltransferase and acyl carrier protein (ACP) during the acyltransfer reaction, the mechanism of ACP recognition by acyltransferase had not been understood in detail. An acyltransferase VinK transfers a dipeptide group between two ACPs, VinL and VinP1LdACP, in vicenistatin biosynthesis. In this study, we attempted to crystallize the VinK-ACP complexes. Because transient enzyme-ACP complexes are difficult to crystallize, we developed a covalent cross-linking strategy to trap the VinK-ACP complexes, allowing the determination of the crystal structure of the VinK-VinL complex. The VinK-VinL complex structure allows the first visualization of the interaction between acyltransferase and ACP and provides detailed mechanistic insights into ACP recognition by acyltransferase.
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| Free Research Field |
農学
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