3HRW
Crystal structure of hemoglobin from mouse (Mus musculus)at 2.8
3HRW の概要
エントリーDOI | 10.2210/pdb3hrw/pdb |
分子名称 | Hemoglobin subunit alpha, Hemoglobin subunit beta-1, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total) |
機能のキーワード | heme, iron, metal-binding, oxygen transport, polymorphism, transport, phosphoprotein |
由来する生物種 | Mus musculus (mouse) 詳細 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 63887.90 |
構造登録者 | |
主引用文献 | Sundaresan, S.S.,Ramesh, P.,Shobana, N.,Vinuchakkaravarthy, T.,Yasien, S.,Ponnuswamy, M.N.G. Crystal structure of hemoglobin from mouse (Mus musculus) compared with those from other small animals and humans. Acta Crystallogr.,Sect.F, 77:113-120, 2021 Cited by PubMed Abstract: Mice (Mus musculus) are nocturnal small animals belonging to the rodent family that live in burrows, an environment in which significantly high CO levels prevail. It is expected that mouse hemoglobin (Hb) plays an important role in their adaptation to living in such a high-CO environment, while many other species cannot. In the present study, mouse Hb was purified and crystallized at a physiological pH of 7 in the orthorhombic space group P222; the crystals diffracted to 2.8 Å resolution. The primary amino-acid sequence and crystal structure of mouse Hb were compared with those of mammalian Hbs in order to investigate the structure-function relationship of mouse Hb. Differences were observed from guinea pig Hb in terms of amino-acid sequence and from cat Hb in overall structure (in terms of r.m.s.d.). The difference in r.m.s.d. from cat Hb may be due to the existence of the molecule in a conformation other than the R-state. Analysis of tertiary- and quaternary-structural features, the α1β2 interface region and the heme environment without any ligands in all four heme groups showed that mouse methemoglobin is in an intermediate state between the R-state and the T-state that is much closer to the R-state conformation. PubMed: 33830076DOI: 10.1107/S2053230X2100306X 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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