1HV4

CRYSTAL STRUCTURE ANALYSIS OF BAR-HEAD GOOSE HEMOGLOBIN (DEOXY FORM)

1HV4 の概要

• エントリーDOI: 10.2210/pdb1hv4/pdb
• 関連するPDBエントリー: 1A4F 1C40
• 分子名称: HEMOGLOBIN ALPHA-A CHAIN, HEMOGLOBIN BETA CHAIN, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: allosteric mechanism, oxygen transport, heme, respiratory protein, oxygen storage-transport complex, oxygen storage/transport
• 由来する生物種: Anser indicus (bar-headed goose); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 131634.08

構造登録者

Liang, Y.,Hua, Z.,Liang, X.,Xu, Q.,Lu, G. (登録日: 2001-01-07, 公開日: 2001-01-17, 最終更新日: 2023-08-09)

主引用文献

Liang, Y.,Hua, Z.,Liang, X.,Xu, Q.,Lu, G.
The crystal structure of bar-headed goose hemoglobin in deoxy form: the allosteric mechanism of a hemoglobin species with high oxygen affinity.
J.Mol.Biol., 313:123-137, 2001

PubMed Abstract: The crystal structure of a high oxygen affinity species of hemoglobin, bar-headed goose hemoglobin in deoxy form, has been determined to a resolution of 2.8 A. The R and R(free) factor of the model are 0.197 and 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 alphabeta 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 A, 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 alpha119 from proline to alanine at the alpha(1)beta(1 )interface in bar-headed goose hemoglobin brings a gap between Ala alpha119 and Leu beta55, the minimum distance between the two residues is 4.66 A. 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 beta146 is at the inositol pentaphosphate binding site and the salt-bridge between His beta146 and Asp beta94 does not exist in the deoxy hemoglobin, which brings the weak chloride-independent Bohr effect to bar-headed goose hemoglobin.

PubMed: 11601851
DOI: 10.1006/jmbi.2001.5028

実験手法

X-RAY DIFFRACTION (2.8 Å)