1H97

Trematode hemoglobin from Paramphistomum epiclitum

1H97 の概要

• エントリーDOI: 10.2210/pdb1h97/pdb
• 分子名称: Globin-3, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: oxygen transport
• 由来する生物種: Paramphistomum epiclitum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34899.33

構造登録者

Pesce, A.,Dewilde, S.,Kiger, L.,Milani, M.,Ascenzi, P.,Marden, M.C.,Van Hauwaert, M.L.,Vanfleteren, J.,Moens, L.,Bolognesi, M. (登録日: 2001-03-02, 公開日: 2001-06-21, 最終更新日: 2024-05-08)

主引用文献

Pesce, A.,Dewilde, S.,Kiger, L.,Milani, M.,Ascenzi, P.,Marden, M.C.,Van, M.L.,Vanfleteren, J.,Moens, L.,Bolognesi, M.
Very High Resolution Structure of a Trematode Hemoglobin Displaying a Tyrb10-Tyre7 Heme Distal Residue Pair and High Oxygen Affinity
J.Mol.Biol., 309:1153-, 2001

PubMed Abstract: 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 residues), which also displays very high oxygen affinity. The oxygenation and carbonylation parameters of wild-type P. epiclitum Hb as well as of single- and double-site mutants, with residue substitutions at positions B10, E7 and E11, have been determined and are discussed here in the light of the protein atomic resolution crystal structure.

PubMed: 11399085
DOI: 10.1006/JMBI.2001.4731

実験手法

X-RAY DIFFRACTION (1.17 Å)