The crystal structure of bar-headed goose hemoglobin in deoxy form: The   allosteric mechanism of a hemoglobin species with high oxygen affinity

doi:10.1006/jmbi.2001.5028

CORC > 北京大学 > 生命科学学院

	The crystal structure of bar-headed goose hemoglobin in deoxy form: The allosteric mechanism of a hemoglobin species with high oxygen affinity
	Liang, YH ; Hua, ZQ ; Liang, X ; Xu, Q ; Lu, GY
刊名	分子生物学杂志
	2001
关键词	crystal structure hemoglobin bar-headed goose allosteric mechanism high-altitude adaptation HIGH-ALTITUDE RESPIRATION STATE DEOXYHEMOGLOBIN COMPONENTS ADAPTATION RESOLUTION GEESE
DOI	10.1006/jmbi.2001.5028
英文摘要	The crystal structure of a high oxygen affinity species of hemoglobin, Engineering and Plant Genetic bar-headed goose hemoglobin in deoxy form, has been determined to a resolution of 2.8 Angstrom. The R and R-free factor of the model are 0.197 and Sciences, Peking University 0.243, respectively. The structure reported here is a special deoxy state of hemoglobin and indicates the differences in allosteric mechanisms between the goose and human hemoglobins. The quaternary structure of the goose deoxy hemoglobin shows obvious differences from that of human deoxy hemoglobin. The rotation angle of one alpha beta dimer relative to its partner in a tetramer molecule from the goose oxy to deoxy hemoglobin is only 4.6 degrees, and the translation is only 0.3 Angstrom, which are much smaller than those in human hemoglobin. In the alpha (1)beta (2) switch region of the goose deoxy hemoglobin, the imidazole ring of His beta (2)97 does not span the side-chain of Thr alpha (1)41 relative to the oxy hemoglobin as in human hemoglobin. And the tertiary structure changes of heme pocket and FG corner are also smaller than that in human hemoglobin. A unique mutation among avian and mammalian Hbs of alpha 119 from proline to alanine at the alpha (1)beta (1) interface in bar-headed goose hemoglobin brings a gap between Ala alpha 119 and Leu beta 55, the minimum distance between the two residues is 4.66 Angstrom. At the entrance to the central cavity around the molecular dyad, some residues of two beta chains form a positively charged groove where the inositol pentaphosphate binds to the hemoglobin. The His beta 146 is at the inositol pentaphosphate binding site and the salt-bridge between His beta 146 and Asp beta 94 does not exist in the deoxy hemoglobin, which brings the weak chloride-independent Bohr effect to bar-headed goose hemoglobin. (C) 2001 Academic Press.; Biochemistry & Molecular Biology; SCI(E); PubMed; 32; ARTICLE; 1; 123-137; 313
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/200533]
专题	生命科学学院
推荐引用方式 GB/T 7714	Liang, YH,Hua, ZQ,Liang, X,et al. The crystal structure of bar-headed goose hemoglobin in deoxy form: The allosteric mechanism of a hemoglobin species with high oxygen affinity[J]. 分子生物学杂志,2001.
APA	Liang, YH,Hua, ZQ,Liang, X,Xu, Q,&Lu, GY.(2001).The crystal structure of bar-headed goose hemoglobin in deoxy form: The allosteric mechanism of a hemoglobin species with high oxygen affinity.分子生物学杂志.
MLA	Liang, YH,et al."The crystal structure of bar-headed goose hemoglobin in deoxy form: The allosteric mechanism of a hemoglobin species with high oxygen affinity".分子生物学杂志 (2001).