| Project/Area Number |
06453219
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Biophysics
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| Research Institution | KYOTO UNIVERSITY |
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Principal Investigator |
MIKI Kunio Grad.School of Science, Kyoto Univ.Prof., 大学院・理学研究科, 教授 (10116105)
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| Co-Investigator(Kenkyū-buntansha) |
KITA Akiko Grad.School of Science, Kyoto Univ.Res.Assoc., 大学院・理学研究科, 助手 (70273430)
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| Project Period (FY) |
1994 – 1995
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| Project Status |
Completed (Fiscal Year 1995)
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| Budget Amount *help |
¥1,900,000 (Direct Cost: ¥1,900,000)
Fiscal Year 1995: ¥1,900,000 (Direct Cost: ¥1,900,000)
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| Keywords | Bioluminescence / Luciferase / EP390 / X-ray Crystal Structure / Three-dimensional Structure / Flavin / FP390 |
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| Research Abstract |
The three-dimensional structure of FP390 protein from a bioluminescent bacterium, Photobacterium phosphoreum, has been determined at 3 A resolution on the basis of diffraction data collected by synchrotron radiation. The crystal structure of this protein was solved by the molecular replacement procedure and refined at 2.7 A resolution to a R value of 24.0%.
The remarkable feature of the structure is that two monomer molecules related by the non-crystallographic two-fold axis to form a dimeric structure. There two Q-flavin molecules in each monomer. One of them is located at the molecular surface and the another is at the dimer interface. The electron density of myristic acids of the Q-flavin at the dimer interface in both monomer are weak and unclear, showing the possibility that Q-flavins bound in this site are not a single species but a mixture of two components.
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