Bishistidyl heme hexacoordination, a key structural property in Drosophila melanogaster hemoglobin

Daniele De Sanctis, Sylvia Dewilde, Clemens Vonrhein, Alessandra Pesce, Luc Moens, Paolo Ascenzi, Thomas Hankeln, Thorsten Burmester, Marco Ponassi, Marco Nardini, Martino Bolognesi

Research output: Contribution to journalArticle

Abstract

Hemoglobins at high concentration have been isolated long ago from some insect larvae living in hypoxic environments. Conversely, a monomeric hemoglobin has been discovered recently in the fruit fly Drosophila melanogaster as intracellular protein expressed both in larvae and in the adult fly. Such a finding indicates that the oxygen supply in insects may be more complex than previously thought, relying not only on O2 diffusion through the tubular tracheal system, but also on carrier-mediated transport and storage. We present here the crystal structure of recombinant D. melanogaster hemoglobin at 1.20 Å resolution. Spectroscopic data show that the protein displays a hexacoordinated heme, whose axial ligands are the proximal and distal His residues. Such bis-His ligation of the heme has sizable effects on the protein local structure. Three protein matrix cavities, comparable in size but not in topological locations with those of sperm whale myoglobin, are spread through the protein matrix; one of these can host a xenon atom. Additionally, D. melanogaster hemoglobin binds one molecule of 3-(cyclohexylamino)propanesulfonic acid (CAPS) buffer at a surface pocket, next to the EF hinge. Despite the high resolution achieved, no sequence/structure features specifically supporting the heme hexa- to pentacoordination transition required for diatomic ligand binding could be recognized.

Original languageEnglish
Pages (from-to)27222-27229
Number of pages8
JournalJournal of Biological Chemistry
Volume280
Issue number29
DOIs
Publication statusPublished - Jul 22 2005

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Drosophila melanogaster
Heme
Structural properties
Hemoglobins
Proteins
Diptera
Larva
Insects
Sperm Whale
Ligands
Oxygen supply
Xenon
Carrier transport
Myoglobin
Hinges
Fruits
Ligation
Fruit
Buffers
Crystal structure

ASJC Scopus subject areas

  • Biochemistry

Cite this

De Sanctis, D., Dewilde, S., Vonrhein, C., Pesce, A., Moens, L., Ascenzi, P., ... Bolognesi, M. (2005). Bishistidyl heme hexacoordination, a key structural property in Drosophila melanogaster hemoglobin. Journal of Biological Chemistry, 280(29), 27222-27229. https://doi.org/10.1074/jbc.M503814200

Bishistidyl heme hexacoordination, a key structural property in Drosophila melanogaster hemoglobin. / De Sanctis, Daniele; Dewilde, Sylvia; Vonrhein, Clemens; Pesce, Alessandra; Moens, Luc; Ascenzi, Paolo; Hankeln, Thomas; Burmester, Thorsten; Ponassi, Marco; Nardini, Marco; Bolognesi, Martino.

In: Journal of Biological Chemistry, Vol. 280, No. 29, 22.07.2005, p. 27222-27229.

Research output: Contribution to journalArticle

De Sanctis, D, Dewilde, S, Vonrhein, C, Pesce, A, Moens, L, Ascenzi, P, Hankeln, T, Burmester, T, Ponassi, M, Nardini, M & Bolognesi, M 2005, 'Bishistidyl heme hexacoordination, a key structural property in Drosophila melanogaster hemoglobin', Journal of Biological Chemistry, vol. 280, no. 29, pp. 27222-27229. https://doi.org/10.1074/jbc.M503814200
De Sanctis, Daniele ; Dewilde, Sylvia ; Vonrhein, Clemens ; Pesce, Alessandra ; Moens, Luc ; Ascenzi, Paolo ; Hankeln, Thomas ; Burmester, Thorsten ; Ponassi, Marco ; Nardini, Marco ; Bolognesi, Martino. / Bishistidyl heme hexacoordination, a key structural property in Drosophila melanogaster hemoglobin. In: Journal of Biological Chemistry. 2005 ; Vol. 280, No. 29. pp. 27222-27229.
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