Crystallographic study of poly-γ-glutamate hydrolase.
| Project/Area Number |
19770093
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Structural biochemistry
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| Research Institution | National Institute of Agrobiological Sciences |
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Principal Investigator |
FUJIMOTO Zui National Institute of Agrobiological Sciences, タンパク質機能研究ユニット, 主任研究員 (20370679)
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| Project Period (FY) |
2007 – 2009
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| Project Status |
Completed (Fiscal Year 2009)
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| Budget Amount *help |
¥3,800,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥600,000)
Fiscal Year 2009: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2008: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2007: ¥1,200,000 (Direct Cost: ¥1,200,000)
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| Keywords | X線結晶解析 / ボリーγーグルタミン酸 / PGA酸加水分解酵素 / 納豆菌 / 酵素反応機構 / X線結晶構造解析 / 双晶 / ポリ-γ-グルタミン酸 |
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| Research Abstract |
Poly-γ-glutamate hydrolase P (PghP) of Bacillus subtilis bacteriophage ΦNIT1 hydrolyzes the γ-glutamyl peptide linkage of extracellular poly-γ-glutamate produced by bacilli. Crystal structure of PghP was determined at a resolution of 1.9 A. Structure of PghP was elucidated as a globular protein with an open α/β mixed core structure and a seven-stranded parallel/anti-parallel β-sheet. Structure analysis demonstrated that PghP had a catalytic center containing a zinc ion and an overall topology resembling mammalian carboxypeptidase A and related enzymes.
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Report
(4 results)
Research Products
(11 results)
