1DM1

2.0 A CRYSTAL STRUCTURE OF THE DOUBLE MUTANT H(E7)V, T(E10)R OF MYOGLOBIN FROM APLYSIA LIMACINA

1DM1 の概要

• エントリーDOI: 10.2210/pdb1dm1/pdb
• 分子名称: MYOGLOBIN, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: globin fold, oxygen storage-transport complex, oxygen storage/transport
• 由来する生物種: Aplysia limacina (slug sea hare)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15938.83

構造登録者

Federici, L.,Savino, C.,Musto, R.,Travaglini-Allocatelli, C.,Cutruzzola, F.,Brunori, M. (登録日: 1999-12-13, 公開日: 2000-06-21, 最終更新日: 2024-02-07)

主引用文献

Federici, L.,Savino, C.,Musto, R.,Travaglini-Allocatelli, C.,Cutruzzola, F.,Brunori, M.
Engineering His(E7) affects the control of heme reactivity in Aplysia limacina myoglobin.
Biochem.Biophys.Res.Commun., 269:58-63, 2000

PubMed Abstract: Aplysia limacina myoglobin lacks the distal histidine (His (E7)) and displays a ligand stabilization mechanism based on Arg(E10). The double mutant Val(E7)His-Arg(E10)Thr has been prepared to engineer the role of His(E7), typical of mammalian myoglobins, in a different globin framework. The 2.0 A crystal structure of Val(E7)His-Arg(E10)Thr met-Mb mutant reveals that the His(E7) side chain points out of the distal pocket, providing an explanation for the observed failure to stabilize the Fe(II) bound oxygen in the ferrous myoglobin. Moreover, spectroscopic analysis together with kinetic data on azide binding to met-myoglobin are reported and discussed in terms of the presence of a water molecule at coordination distance from the heme iron.

PubMed: 10694477
DOI: 10.1006/bbrc.2000.2259

実験手法

X-RAY DIFFRACTION (1.99 Å)