1kfr
|
Structural plasticity in the eight-helix fold of a trematode hemoglobin
OverviewOverview
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 A resolution (orthorhombic space group P2(1)2(1)2(1)). In the present communication, the three-dimensional structure of wild-type P. epiclitum haemoglobin is reported at 1.85 A resolution in a monoclinic crystal form (R factor = 16.1%, R(free) = 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.
About this StructureAbout this Structure
1KFR is a Single protein structure of sequence from Paramphistomum epiclitum with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structural plasticity in the eight-helix fold of a trematode haemoglobin., Milani M, Pesce A, Dewilde S, Ascenzi P, Moens L, Bolognesi M, Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):719-22. Epub 2002, Mar 22. PMID:11914507
Page seeded by OCA on Thu Feb 21 13:33:40 2008