Dynamics of hydrogen bond network among the side chains in the active site of enzyme revealed by NMR deuterium isotope shift
| Project/Area Number |
26650023
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Structural biochemistry
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| Research Institution | Hiroshima University |
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Principal Investigator |
Shin-ichi Tate 広島大学, 理学(系)研究科(研究院), 教授 (20216998)
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| Project Period (FY) |
2014-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2015: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2014: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | NMR / プロリン異性化酵素 / 重水素同位体シフト / 安定同位体 / タンパク質 / 酵素 / 水素結合 / タンパク質構造動態 / 同位体効果 / 化学シフト / 酵素活性部位 |
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| Outline of Final Research Achievements |
NMR isotope shifts caused by the proton/deuteron change were exploited to reveal the relations between the proline isomerase activity of Pin1 and the hydrogen bond network formed in the active site. The isotope shift was used to quantitatively elucidate the changes in the strength of the hydrogen bonds in the network. We made three different mutants having amino acid changes to C113 in the active site of the isomerase domain of Pin1, PPIase. In addition, C138 mutation was applied to see the distal effect on the hydrogen bond network.
Combined the results from the analyses on the different mutants made the role of the hydrogen bond network in the PPIase active site clearer.
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Report
(3 results)
Research Products
(24 results)
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[Journal Article] Allosteric breakage to the hydrogen bond within the dual-histidine motif in the active site of human Pin1 PPIase2015
Author(s)
Wang,J., Tochio,N., Kawasaki,R., Tamari,Y., Xu,N., Uewaki,J., Utsunomiya-Tate,N., Tate,S.
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Journal Title
Biochemistry
Volume: 54
Issue: 33
Pages: 5242-5253
DOI
Related Report
Peer Reviewed / Acknowledgement Compliant
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[Journal Article] Coating the outer surface of glass nanopipette with chlorobenzene-terminated polysiloxane2015
Author(s)
Takami,T., Ojiro,Y., Ogawa,S., Takaku,Y., Ogawa,Y., Saito,M., Matuoka,H., Tate,S.
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Journal Title
e-J.Surf.Sci. Nanotech
Volume: 13
Pages: 79-84
NAID
Related Report
Peer Reviewed
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[Journal Article] The C113D mutation in human Pin1 causes allosteric structural changes in the phosphate binding pocket of the PPIase domain through the tug of war in the dual-histidine motif2014
Author(s)
Xu,N., Tochio,N., Wang,J., Tamari,Y., Uewaki,J., Utsunomiya-Tate,N., Igarashi,K., Shiraki,T, Kobayashi,N., Tate,S.
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Journal Title
Biochemistry
Volume: 53
Issue: 34
Pages: 5568-5578
DOI
Related Report
Peer Reviewed / Acknowledgement Compliant
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