1T1N

CRYSTAL STRUCTURE OF CARBONMONOXY HEMOGLOBIN

1T1N の概要

• エントリーDOI: 10.2210/pdb1t1n/pdb
• 分子名称: PROTEIN (HEMOGLOBIN), PROTOPORPHYRIN IX CONTAINING FE, CARBON MONOXIDE, ... (5 entities in total)
• 機能のキーワード: oxygen transport, hemoglobin
• 由来する生物種: Trematomus newnesi (dusky notothen); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 33238.70

構造登録者

Mazzarella, L.,Vitagliano, L.,Savino, C.,Zagari, A. (登録日: 1999-03-05, 公開日: 1999-04-29, 最終更新日: 2024-10-30)

主引用文献

Mazzarella, L.,D'Avino, R.,di Prisco, G.,Savino, C.,Vitagliano, L.,Moody, P.C.E.,Zagari, A.
Crystal structure of Trematomus newnesi haemoglobin re-opens the root effect question.
J.Mol.Biol., 287:897-906, 1999

PubMed Abstract: As new structural data have become available, somewhat contrasting explanations of the Root effect in fish haemoglobins (Hb) have been provided. Hb 1 of the Antarctic fish Trematomus newnesi has a nearly pH-independent oxygen affinity, in spite of 95 % sequence identity with Hb 1 of Trematomus (previously named Pagothenia) bernacchii that has a strong Root effect. Here, the 2.2 A R-state structure of Trematomus newnesi Hb 1 is presented. The structure is similar to that of Root effect fish Hbs from Spot and T. bernacchii, suggesting that the differences in the pH dependence cannot be related to the modulation of the R-state. In comparison to T. bernacchii Hb 1, the role of the three mutations Thr41 (C6)alpha-->Ile, Ala97 (G3)alpha-->Ser and His41 (C7)beta-->Tyr at the alpha1beta2-interface is discussed.

PubMed: 10222199
DOI: 10.1006/jmbi.1999.2632

実験手法

X-RAY DIFFRACTION (2.2 Å)