3PEL

Structure of Greyhound Hemoglobin: Origin of High Oxygen Affinity

「3N48」から置き換えられました

3PEL の概要

• エントリーDOI: 10.2210/pdb3pel/pdb
• 分子名称: Hemoglobin subunit alpha, Hemoglobin subunit beta, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• 機能のキーワード: globin fold, oxygen/co2 transport, heme binding, red blood cells, oxygen transport
• 由来する生物種: Canis lupus familiaris (dogs); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32493.64

構造登録者

Bhatt, V.S.,Zaldivar-Lopez, S.,Harris, D.R.,Couto, C.G.,Wang, P.G.,Palmer, A.F. (登録日: 2010-10-26, 公開日: 2010-11-03, 最終更新日: 2023-09-06)

主引用文献

Bhatt, V.S.,Zaldivar-Lopez, S.,Harris, D.R.,Couto, C.G.,Wang, P.G.,Palmer, A.F.
Structure of Greyhound hemoglobin: origin of high oxygen affinity.
Acta Crystallogr.,Sect.D, 67:395-402, 2011

PubMed Abstract: This study presents the crystal structure of Greyhound hemoglobin (GrHb) determined to 1.9 Å resolution. GrHb was found to crystallize with an α₁β₁ dimer in the asymmetric unit and belongs to the R2 state. Oxygen-affinity measurements combined with the fact that GrHb crystallizes in the R2 state despite the high-salt conditions used for crystallization strongly indicate that GrHb can serve as a model high-oxygen-affinity hemoglobin (Hb) for higher mammals, especially humans. Structural analysis of GrHb and its comparison with the R2-state of human Hb revealed several regions that can potentially contribute to the high oxygen affinity of GrHb and serve to rationalize the additional stability of the R2-state of GrHb. A previously well studied hydrophobic cluster of bar-headed goose Hb near α119 was also incorporated in the comparison between GrHb and human Hb. Finally, a structural comparison with generic dog Hb and maned wolf Hb was conducted, revealing that in contrast to GrHb these structures belong to the R state of Hb and raising the intriguing possibility of an additional allosteric factor co-purifying with GrHb that can modulate its quaternary structure.

PubMed: 21543841
DOI: 10.1107/S0907444911006044

実験手法

X-RAY DIFFRACTION (1.9 Å)