1KFR

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

1KFR の概要

• エントリーDOI: 10.2210/pdb1kfr/pdb
• 関連するPDBエントリー: 1H97
• 分子名称: Hemoglobin, SULFATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• 機能のキーワード: hemoglobin, oxygen storage-transport complex, oxygen storage/transport
• 由来する生物種: Paramphistomum epiclitum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17473.60

構造登録者

Milani, M.,Pesce, A.,Dewilde, S.,Ascenzi, P.,Moens, L.,Bolognesi, M. (登録日: 2001-11-22, 公開日: 2002-04-24, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.85 Å)