The 2.0.ANGS. crystal structure of cyanide metmyoglobin reconstituted with 5,10,15,20-tetrapropylhemin.
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概要
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Sperm whale metmyoglobin reconstituted with 5,10,15,20-tetrapropylhemin was crystallized in the space group <I>P</I>2<SUB>1</SUB>2<SUB>1</SUB>2<SUB>1</SUB>, which was different from the space group <I>P</I>2<SUB>1</SUB> of the native. The crystal structure of the reconstituted metmyoglobin was determined by the molecular replacement method. The atomic coordinates were refined to <I>R</I>=0.209 at 2.0 Å resolution. The overall structure is essentially the same as that of the native. The pronounced structural change is observed in the side-chain orientation of Arg 45 moving to the surface of the molecule. This conformational change may reflect a side-chain fluctuation that allows the small ligands to approach the heme pocket from the outside of the protein. The porphyrin ring does not rotate freely about the Fe–N<SUP>ε</SUP> (His 93) bond in the crystalline state, although temperature-dependent NMR spectra suggest its free rotation in solution.
- 公益社団法人 日本化学会の論文
著者
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KATSUBE Yukiteru
Institute for Protein Research, Osaka University
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Neya Saburo
Department Of Physical Chemistry Faculty Of Pharmaceutical Sciences Chiba University
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Hata Yasuo
Institute For Chemical Research Kyoto University
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Hata Tadashi
Analytical And Metabolic Research Laboratories Sankyo Co. Ltd.
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Katsube Yukiteru
Institute For Protein Research Osaka University
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Tanaka Nobuo
Department Of Agro-environmental Sciences Graduate School Of Bioresource And Bioenvironmental Scienc
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Sato Takao
Department Of Biological Science And Technology Faculty Of Engineering The University Of Tokushima
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Funasaki Noriaki
Department of Physical Chemistry, Kyoto Pharmaceutical University
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Funasaki Noriaki
Department of Biophysical Chemistry, Kyoto Pharmaceutical University
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HATA Tadashi
Analytical and Metabolic Research Laboratories, Sankyo Co., Ltd.
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Katsube Yukiteru
Institute for Protein Research
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Hata Tadashi
Analytical and Metabolic Laboratories, Sankyo Co., Ltd.
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