1995 Fiscal Year Final Research Report Summary

Studies on Molecular Mechanism of Bioluminescence

Research Project

Project/Area Number	06453219
Research Category	Grant-in-Aid for General Scientific Research (B)
Allocation Type	Single-year Grants
Research Field	Biophysics
Research Institution	KYOTO UNIVERSITY
Principal Investigator	MIKI Kunio Grad.School of Science, Kyoto Univ.Prof., 大学院・理学研究科, 教授 (10116105)
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)
Project Period (FY)	1994 – 1995
Keywords	Bioluminescence / Luciferase / EP390 / X-ray Crystal Structure / Three-dimensional Structure / Flavin
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.

(6 results)