6J79

Fusion protein of heme oxygenase-1 and NADPH-cytochrome P450 reductase (13aa)

Summary for 6J79

• Entry DOI: 10.2210/pdb6j79/pdb
• Descriptor: Heme oxygenase 1,NADPH--cytochrome P450 reductase, FLAVIN-ADENINE DINUCLEOTIDE, FLAVIN MONONUCLEOTIDE, ... (5 entities in total)
• Functional Keywords: fusion protein, redox complex, oxidoreductase
• Biological source: Rattus norvegicus (Rat); More
• Total number of polymer chains: 2
• Total formula weight: 202396.87

Authors

Sugishima, M.,Wada, K. (deposition date: 2019-01-17, release date: 2019-04-10, Last modification date: 2023-11-22)

Primary citation

Sugishima, M.,Sato, H.,Wada, K.,Yamamoto, K.
Crystal structure of a NADPH-cytochrome P450 oxidoreductase (CYPOR) and heme oxygenase 1 fusion protein implies a conformational change in CYPOR upon NADPH/NADP+binding.
Febs Lett., 593:868-875, 2019

PubMed Abstract: 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 Å. Here, we determined the crystal structure of the fusion protein of open-conformation stabilized CYPOR and heme-HMOX1 at 3.25 Å 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.

PubMed: 30883732
DOI: 10.1002/1873-3468.13360

Experimental method

X-RAY DIFFRACTION (3.331 Å)