Structural study of D-Ala-D-Ala ligase to develop new antibiotics
| Project/Area Number |
20790035
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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 |
Physical pharmacy
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| Research Institution | Hiroshima University |
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Principal Investigator |
MATOBA Yasuyuki Hiroshima University, 大学院・医歯薬学総合研究科, 准教授 (90363051)
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| Project Period (FY) |
2008 – 2009
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| Project Status |
Completed (Fiscal Year 2009)
|
| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2009: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2008: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | 構造生物 / 抗生物質 / 酵素 / ドラッグデザイン / 構造生物学 |
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| Research Abstract |
The aim of this study is to clarify the structural basis of D-cycloserine (DCS) resistance of DCS-resistant D-Ala-D-Ala ligase. From the amino acid sequence analysis, it was found that Tyr residue in the substrate-binding pocket, which is conserved among DCS-sensitive D-Ala-D-Ala ligases, is replaced by Phe residue in the DCS-resistant D-Ala-D-Ala ligase. In this study, it was proved that the Phe residue contributes to the DCS-resistance.
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Report
(3 results)
Research Products
(19 results)
