1dm1
From Proteopedia
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2.0 A CRYSTAL STRUCTURE OF THE DOUBLE MUTANT H(E7)V, T(E10)R OF MYOGLOBIN FROM APLYSIA LIMACINA
Overview
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.
About this Structure
1DM1 is a Single protein structure of sequence from Aplysia limacina with HEM as ligand. Full crystallographic information is available from OCA.
Reference
Engineering His(E7) affects the control of heme reactivity in Aplysia limacina myoglobin., Federici L, Savino C, Musto R, Travaglini-Allocatelli C, Cutruzzola F, Brunori M, Biochem Biophys Res Commun. 2000 Mar 5;269(1):58-63. PMID:10694477
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