4G51

Crystallographic analysis of the interaction of nitric oxide with hemoglobin from Trematomus bernacchii in the T quaternary structure (fully ligated state).

4G51 の概要

• エントリーDOI: 10.2210/pdb4g51/pdb
• 分子名称: Hemoglobin subunit alpha, Hemoglobin subunit beta, NITRIC OXIDE, ... (5 entities in total)
• 機能のキーワード: all alpha proteins, oxygen transporter, n-terminal acetylated serine, oxygen transport
• 由来する生物種: Trematomus bernacchii (rockcod); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 66259.25

構造登録者

Merlino, A.,Balsamo, A.,Pica, A.,Mazzarella, L.,Vergara, A. (登録日: 2012-07-17, 公開日: 2013-01-16, 最終更新日: 2024-11-06)

主引用文献

Merlino, A.,Fuchs, M.R.,Pica, A.,Balsamo, A.,Dworkowski, F.S.,Pompidor, G.,Mazzarella, L.,Vergara, A.
Selective X-ray-induced NO photodissociation in haemoglobin crystals: evidence from a Raman-assisted crystallographic study.
Acta Crystallogr.,Sect.D, 69:137-140, 2013

PubMed Abstract: Despite their high physiological relevance, haemoglobin crystal structures with NO bound to haem constitute less than 1% of the total ligated haemoglobins (Hbs) deposited in the Protein Data Bank. The major difficulty in obtaining NO-ligated Hbs is most likely to be related to the oxidative denitrosylation caused by the high reactivity of the nitrosylated species with O(2). Here, using Raman-assisted X-ray crystallography, it is shown that under X-ray exposure (at four different radiation doses) crystals of nitrosylated haemoglobin from Trematomus bernacchii undergo a transition, mainly in the β chains, that generates a pentacoordinate species owing to photodissociation of the Fe-NO bond. These data provide a physical explanation for the low number of nitrosylated Hb structures available in the literature.

PubMed: 23275172
DOI: 10.1107/S0907444912042229

実験手法

X-RAY DIFFRACTION (2.5 Å)