3HRW
Crystal structure of hemoglobin from mouse (Mus musculus)at 2.8
Summary for 3HRW
| Entry DOI | 10.2210/pdb3hrw/pdb |
| Descriptor | Hemoglobin subunit alpha, Hemoglobin subunit beta-1, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total) |
| Functional Keywords | heme, iron, metal-binding, oxygen transport, polymorphism, transport, phosphoprotein |
| Biological source | Mus musculus (mouse) More |
| Total number of polymer chains | 4 |
| Total formula weight | 63887.90 |
| Authors | Sundaresan, S.S.,Ramesh, P.,Ponnuswamy, M.N. (deposition date: 2009-06-10, release date: 2009-06-23, Last modification date: 2023-11-01) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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