1DM1

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

Summary for 1DM1

• Entry DOI: 10.2210/pdb1dm1/pdb
• Descriptor: MYOGLOBIN, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: globin fold, oxygen storage-transport complex, oxygen storage/transport
• Biological source: Aplysia limacina (slug sea hare)
• Total number of polymer chains: 1
• Total formula weight: 15938.83

Authors

Federici, L.,Savino, C.,Musto, R.,Travaglini-Allocatelli, C.,Cutruzzola, F.,Brunori, M. (deposition date: 1999-12-13, release date: 2000-06-21, Last modification date: 2024-02-07)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.99 Å)