期刊
FEBS LETTERS
卷 593, 期 8, 页码 868-875出版社
WILEY
DOI: 10.1002/1873-3468.13360
关键词
electron transfer; protein-protein interaction; conformation change; X-ray crystallography
资金
- JSPS KAKENHI [16K07280, 25840026]
- Takeda Science Foundation
- Protein Research Foundation
- Platform Project for Supporting Drug Discovery and Life Science Research [Basis for Supporting Innovative Drug Discovery and Life Science Research (BINDS)] from AMED [JP17am0101072, JP18am0101072]
- Grants-in-Aid for Scientific Research [16K07280, 25840026] Funding Source: KAKEN
Heme oxygenase-1 (HMOX1) catalyzes heme degradation utilizing reducing equivalents supplied from NADPH-cytochrome P450 reductase (CYPOR). Recently, we determined the complex structure of NADP(+)-bound open-conformation stabilized CYPOR and heme-HMOX1, but the resolution was limited to 4.3 angstrom. Here, we determined the crystal structure of the fusion protein of open-conformation stabilized CYPOR and heme-HMOX1 at 3.25 angstrom resolution. Unexpectedly, no NADP(+) was bound to this fusion protein in the crystal. Structural comparison of the NADP(+)-bound complex and the NADP(+)-free fusion protein suggests that NADP(+) binding regulates the conformational change in the FAD-binding domain of CYPOR. As a result of this change, the FMN-binding domain of CYPOR approaches heme-bound HMOX1 upon NADP(+) binding to enhance the electron-transfer efficiency from FMN to heme.
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