Volume 58, Issue 4 pp. 719-722

Structural plasticity in the eight-helix fold of a trematode haemoglobin

First published: 16 June 2004
Martino Bolognesi, e-mail: [email protected]

Abstract

The three-dimensional structure of recombinant haemoglobin from the trematode Paramphistomum epiclitum, displaying the highest oxygen affinity so far observed for (non)vertebrate haemoglobins, has previously been determined at 1.17 Å resolution (orthorhombic space group P212121). In the present communication, the three-dimensional structure of wild-type P. epiclitum haemoglobin is reported at 1.85 Å resolution in a monoclinic crystal form (R factor = 16.1%, Rfree = 22.0%). Comparison of P. epiclitum (recombinant versus wild-type ferric Hb) structures in the two crystal forms shows structural differences in the haem proximal and distal sites which have not been reported for other known haemoglobin structures previously.

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