1h97

From Proteopedia

Revision as of 19:48, 29 October 2007

TREMATODE HEMOGLOBIN FROM PARAMPHISTOMUM EPICLITUM

Overview

Monomeric hemoglobin from the trematode Paramphistomum epiclitum displays, very high oxygen affinity (P(50)<0.001 mm Hg) and an unusual heme distal, site containing tyrosyl residues at the B10 and E7 positions. The crystal, structure of aquo-met P. epiclitum hemoglobin, solved at 1.17 A resolution, via multiwavelength anomalous dispersion techniques (R-factor=0.121), shows that the heme distal site pocket residue TyrB10 is engaged in, hydrogen bonding to the iron-bound ligand. By contrast, residue TyrE7 is, unexpectedly locked next to the CD globin region, in a conformation, unsuitable for heme-bound ligand stabilisation. Such structural, organization of the E7 distal residue differs strikingly from that, observed in the nematode Ascaris suum hemoglobin (bearing TyrB10 and GlnE7, ... [(full description)]

About this Structure

1H97 is a [Single protein] structure of sequence from [Paramphistomum epiclitum] with SO4 and HEM as [ligands]. Full crystallographic information is available from [OCA].

Reference

Very high resolution structure of a trematode hemoglobin displaying a TyrB10-TyrE7 heme distal residue pair and high oxygen affinity., Pesce A, Dewilde S, Kiger L, Milani M, Ascenzi P, Marden MC, Van Hauwaert ML, Vanfleteren J, Moens L, Bolognesi M, J Mol Biol. 2001 Jun 22;309(5):1153-64. PMID:11399085

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