1KFR

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

Summary for 1KFR

• Entry DOI: 10.2210/pdb1kfr/pdb
• Related: 1H97
• Descriptor: Hemoglobin, SULFATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• Functional Keywords: hemoglobin, oxygen storage-transport complex, oxygen storage/transport
• Biological source: Paramphistomum epiclitum
• Total number of polymer chains: 1
• Total formula weight: 17473.60

Authors

Milani, M.,Pesce, A.,Dewilde, S.,Ascenzi, P.,Moens, L.,Bolognesi, M. (deposition date: 2001-11-22, release date: 2002-04-24, Last modification date: 2024-02-07)

Primary citation

Milani, M.,Pesce, A.,Dewilde, S.,Ascenzi, P.,Moens, L.,Bolognesi, M.
Structural plasticity in the eight-helix fold of a trematode haemoglobin.
Acta Crystallogr.,Sect.D, 58:719-722, 2002

PubMed 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 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.

PubMed: 11914507
DOI: 10.1107/S0907444902001865

Experimental method

X-RAY DIFFRACTION (1.85 Å)