The 109 residue nerve tissue minihemoglobin from Cerebratulus lacteus highlights striking structural plasticity of the α-helical globin fold

Alessandra Pesce, Marco Nardini, Sylvia Dewilde, Eva Geuens, Kiyoshi Yamauchi, Paolo Ascenzi, Austen F. Riggs, Luc Moens, Martino Bolognesi

Research output: Contribution to journalArticlepeer-review

Abstract

A very short hemoglobin (CerHb; 109 amino acids) binds O2 cooperatively in the nerve tissue of the nemertean worm Cerebratulus lacteus to sustain neural activity during anoxia. Sequence analysis suggests that CerHb tertiary structure may be unique among the known globin fold evolutionary variants. The X-ray structure of oxygenated CerHb (R factor 15.3%, at 1.5 Å resolution) displays deletion of the globin N-terminal A helix, an extended GH region, a very short H helix, and heme solvent shielding based on specific aromatic residues. The heme-bound O2 is stabilized by hydrogen bonds to the distal TyrB10-GlnE7 pair. Ligand access to heme may take place through a wide protein matrix tunnel connecting the distal site to a surface cleft located between the E and H helices.

Original languageEnglish
Pages (from-to)725-735
Number of pages11
JournalStructure
Volume10
Issue number5
DOIs
Publication statusPublished - 2002

Keywords

  • Globin fold plasticity
  • Nerve tissue minihemoglobin
  • Oxygen binding
  • Oxygenated hemoglobin
  • Protein cavities
  • X-ray crystallography

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

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