A novel two-over-two α-helical sandwich fold is characteristic of the truncated hemoglobin family

Alessandra Pesce, Manon Couture, Sylvia Dewilde, Michel Guertin, Kiyoshi Yamauchi, Paolo Ascenzi, Luc Moens, Martino Bolognesi

Research output: Contribution to journalArticle

200 Citations (Scopus)

Abstract

Small hemoproteins displaying amino acid sequences 20-40 residues shorter than (non-)vertebrate hemoglobins (Hbs) have recently been identified in several pathogenic and non-pathogenic unicellular organisms, and named 'truncated hemoglobins' (trHbs). They have been proposed to be involved not only in oxygen transport but also in other biological functions, such as protection against reactive nitrogen species, photosynthesis or to act as terminal oxidases. Crystal structures of trHbs from the ciliated protozoan Paramecium caudatum and the green unicellular alga Chlamydomonas eugametos show that the tertiary structure of both proteins is based on a 'two-over-two' α-helical sandwich, reflecting an unprecedented editing of the classical 'three-over-three' a-helical globin fold. Based on specific Gly-Gly moths the tertiary structure accommodates the deletion of the N-terminal A-helix and replacement of the crucial heme-binding F-helix with an extended polypeptide loop. Additionally, concerted structural modifications allow burying of the heme group and define the distal site, which hosts a TyrB10, GlnE7 residue pair. A set of structural and amino acid sequence consensus rules for stabilizing the fold and the bound heme in the trHbs homology subfamily is deduced.

Original languageEnglish
Pages (from-to)2424-2434
Number of pages11
JournalEMBO Journal
Volume19
Issue number11
Publication statusPublished - Jun 1 2000

Fingerprint

Truncated Hemoglobins
Heme
Amino Acid Sequence
Paramecium caudatum
Chlamydomonas
Reactive Nitrogen Species
Amino Acids
Chlorophyta
Globins
Photosynthesis
Moths
Algae
Tertiary Protein Structure
Vertebrates
Oxidoreductases
Hemoglobins
Crystal structure
Oxygen
Peptides
Proteins

Keywords

  • Chloroplast hemoglobin
  • Globin-fold evolution
  • Helical fold
  • Hemoglobins
  • Paramecium hemoglobin

ASJC Scopus subject areas

  • Genetics
  • Cell Biology

Cite this

Pesce, A., Couture, M., Dewilde, S., Guertin, M., Yamauchi, K., Ascenzi, P., ... Bolognesi, M. (2000). A novel two-over-two α-helical sandwich fold is characteristic of the truncated hemoglobin family. EMBO Journal, 19(11), 2424-2434.

A novel two-over-two α-helical sandwich fold is characteristic of the truncated hemoglobin family. / Pesce, Alessandra; Couture, Manon; Dewilde, Sylvia; Guertin, Michel; Yamauchi, Kiyoshi; Ascenzi, Paolo; Moens, Luc; Bolognesi, Martino.

In: EMBO Journal, Vol. 19, No. 11, 01.06.2000, p. 2424-2434.

Research output: Contribution to journalArticle

Pesce, A, Couture, M, Dewilde, S, Guertin, M, Yamauchi, K, Ascenzi, P, Moens, L & Bolognesi, M 2000, 'A novel two-over-two α-helical sandwich fold is characteristic of the truncated hemoglobin family', EMBO Journal, vol. 19, no. 11, pp. 2424-2434.
Pesce A, Couture M, Dewilde S, Guertin M, Yamauchi K, Ascenzi P et al. A novel two-over-two α-helical sandwich fold is characteristic of the truncated hemoglobin family. EMBO Journal. 2000 Jun 1;19(11):2424-2434.
Pesce, Alessandra ; Couture, Manon ; Dewilde, Sylvia ; Guertin, Michel ; Yamauchi, Kiyoshi ; Ascenzi, Paolo ; Moens, Luc ; Bolognesi, Martino. / A novel two-over-two α-helical sandwich fold is characteristic of the truncated hemoglobin family. In: EMBO Journal. 2000 ; Vol. 19, No. 11. pp. 2424-2434.
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