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High-resolution X-ray crystal structure of cytochrome ${it b$_{5}$}$ from porcine liver

Hirano, Yu; Kimura, Shigenobu*; Tamada, Taro

Mammalian microsomal cytochrome ${it b$_{5}$}$ (b5) is a hemoprotein which anchored to the membrane of the endoplasmic reticulum and it is involved in various electron transfer reactions, such as lipid unsaturation, cholesterol synthesis and drug metabolism. The 1.5 ${AA}$, structure of b5 from bovine liver reveals that acidic residues located in the vicinity of heme play a role in interaction with electron transfer partners. To further understand the electron transfer mechanism based on the precious structural information, we attempted the structure determination above 1 ${AA}$, resolution of both oxidized (OX) and reduced (RD) form of porcine liver b5. We obtained four types of b5 crystals, OX with/without calcium ion (Ca$$^{2+}$$) and RD with/without Ca$$^{2+}$$, and then collected each dataset above 1 ${AA}$, resolution, 0.85 ${AA}$, (OX + Ca$$^{2+}$$), 0.93 ${AA}$,(OX - Ca$$^{2+}$$), 0.85 ${AA}$, (RD + Ca$$^{2+}$$), and 0.95 ${AA}$, (RD - Ca$$^{2+}$$). In the both structures of OX and RD form with Ca$$^{2+}$$, two glutamate located in the vicinity of heme participated in the recognition of Ca$$^{2+}$$. From the comparison among four structures, we confirmed that the structural difference between with and without Ca$$^{2+}$$ (RMSD: 0.61-0.65 ${AA}$) is larger than that between OX and RD form (RMSD: 0.12-0.23 ${AA}$).

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