2VYW

Hemoglobin (Hb2) from trematode Fasciola hepatica

Summary for 2VYW

• Entry DOI: 10.2210/pdb2vyw/pdb
• Descriptor: HEMOGLOBIN, PROTOPORPHYRIN IX CONTAINING FE, OXYGEN MOLECULE, ... (4 entities in total)
• Functional Keywords: hemoglobin, trematode, oxygen binding
• Biological source: FASCIOLA HEPATICA
• Total number of polymer chains: 1
• Total formula weight: 17232.53

Authors

Dewilde, S.,Ioanitescu, A.I.,Kiger, L.,Gilany, K.,Marden, M.C.,Van Doorslaer, S.,Vercruysse, J.,Pesce, A.,Nardini, M.,Bolognesi, M.,Moens, L. (deposition date: 2008-07-29, release date: 2008-08-12, Last modification date: 2023-12-13)

Primary citation

Dewilde, S.,Ioanitescu, A.I.,Kiger, L.,Gilany, K.,Marden, M.C.,Van Doorslaer, S.,Vercruysse, J.,Pesce, A.,Nardini, M.,Bolognesi, M.,Moens, L.
The Hemoglobins of the Trematodes Fasciola Hepatica and Paramphistomum Epiclitum: A Molecular Biological, Physico-Chemical, Kinetic, and Vaccination Study.
Protein Sci., 17:1653-, 2008

PubMed Abstract: The trematode Fasciola hepatica (Fa.he.) is a common parasite of human and livestock. The hemoglobin (Hb) of Fa.he., a potential immunogen, was chosen for characterization in the search for an effective vaccine. Characterization of trematode Hbs show that they are intracellular single-domain globins with the following remarkable features: (1) Fa.he. expresses two Hb isoforms that differ at two amino acid sites (F1: 119Y/123Q; F2: 119F/123L). Both isoforms are monoacetylated at their N-termini; (2) the genes coding for Fa.he. and Paramphistomum epiclitum (Pa.ep.) Hbs are interrupted by two introns at the conserved positions B12.2 and G7.0.; (3) UV/VIS and resonance Raman spectroscopy identify the recombinant Fa.he. HbF2 as a pentacoordinated high-spin ferrous Hb; (4) electron paramagnetic resonance spectroscopy of cyano-met Fa.he. HbF2 proves that the endogenously bound imidazole has no imidazolate character; (5) the major structural determinants of the globin fold are present, they contain a TyrB10/TyrE7 residue pair on the distal side. Although such distal-site pair is a signature for high oxygen affinity, as shown for Pa.ep. Hb, the oxygen-binding rate parameters for Fa.he. Hb are intermediate between those of myoglobin and those of other trematode Hbs; (6) the three-dimensional structure of recombinant Fa.he. HbF2 from this study closely resembles the three-dimensional structure of Pa.ep. determined earlier. The set of distal-site polar interactions observed in Pa.ep. Hb is matched with small but significant structural adjustments; (7) despite the potential immunogenic character of the fluke Hb, vaccination of calves with recombinant Fa.he. HbF2 failed to promote protection against parasitic infection.

PubMed: 18621914
DOI: 10.1110/PS.036558.108

Experimental method

X-RAY DIFFRACTION (1.8 Å)