2UYD
Crystal structure of the SmHasA mutant H83A
2UYD の概要
エントリーDOI | 10.2210/pdb2uyd/pdb |
関連するPDBエントリー | 1B2V 1DK0 1DKH 1YBJ 2CN4 |
分子名称 | HEMOPHORE HASA, PROTOPORPHYRIN IX CONTAINING FE, ZINC ION, ... (5 entities in total) |
機能のキーワード | heme, iron, hemophore, heme binding, iron ligation, metal-binding, heme acquisition system, metal-binding protein, metal binding protein |
由来する生物種 | SERRATIA MARCESCENS |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 20479.42 |
構造登録者 | Czjzek, M.,Caillet-Saguy, C.,Fournelle, A.,Guigliarelli, B.,Izadi-Pruneyre, N.,Lecroisey, A. (登録日: 2007-04-04, 公開日: 2007-12-25, 最終更新日: 2023-12-13) |
主引用文献 | Caillet-Saguy, C.,Turano, P.,Piccioli, M.,Lukat-Rodgers, G.S.,Czjzek, M.,Guigliarelli, B.,Izadi-Pruneyre, N.,Rodgers, K.R.,Delepierre, M.,Lecroisey, A. Deciphering the Structural Role of Histidine 83 for Heme Binding in Hemophore Hasa. J.Biol.Chem., 283:5960-, 2008 Cited by PubMed Abstract: Heme carrier HasA has a unique type of histidine/tyrosine heme iron ligation in which the iron ion is in a thermally driven two spin states equilibrium. We recently suggested that the H-bonding between Tyr75 and the invariantly conserved residue His83 modulates the strength of the iron-Tyr75 bond. To unravel the role of His83, we characterize the iron ligation and the electronic properties of both wild type and H83A mutant by a variety of spectroscopic techniques. Although His83 in wild type modulates the strength of the Tyr-iron bond, its removal causes detachment of the tyrosine ligand, thus giving rise to a series of pH-dependent equilibria among species with different axial ligation. The five coordinated species detected at physiological pH may represent a possible intermediate of the heme transfer mechanism to the receptor. PubMed: 18162469DOI: 10.1074/JBC.M703795200 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.7 Å) |
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