3WFW

Crystal Structure of the Closed Form of the HGbRL's Globin Domain

3WFW の概要

• エントリーDOI: 10.2210/pdb3wfw/pdb
• 関連するPDBエントリー: 3WFX
• 分子名称: Hemoglobin-like flavoprotein fused to Roadblock/LC7 domain, PROTOPORPHYRIN IX CONTAINING FE, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
• 機能のキーワード: globin, signalling, closed form, oxygen transport
• 由来する生物種: Methylacidiphilum infernorum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17415.17

構造登録者

Teh, A.H. (登録日: 2013-07-24, 公開日: 2014-08-06, 最終更新日: 2024-03-20)

主引用文献

Teh, A.H.,Saito, J.A.,Najimudin, N.,Alam, M.
Open and Lys-His Hexacoordinated Closed Structures of a Globin with Swapped Proximal and Distal Sites.
Sci Rep, 5:11407-11407, 2015

PubMed Abstract: Globins are haem-binding proteins with a conserved fold made up of α-helices and can possess diverse properties. A putative globin-coupled sensor from Methylacidiphilum infernorum, HGbRL, contains an N-terminal globin domain whose open and closed structures reveal an untypical dimeric architecture. Helices E and F fuse into an elongated helix, resulting in a novel site-swapped globin fold made up of helices A-E, hence the distal site, from one subunit and helices F-H, the proximal site, from another. The open structure possesses a large cavity binding an imidazole molecule, while the closed structure forms a unique Lys-His hexacoordinated species, with the first turn of helix E unravelling to allow Lys52(E10) to bind to the haem. Ligand binding induces reorganization of loop CE, which is stabilized in the closed form, and helix E, triggering a large conformational movement in the open form. These provide a mechanical insight into how a signal may be relayed between the globin domain and the C-terminal domain of HGbRL, a Roadblock/LC7 domain. Comparison with HGbI, a closely related globin, further underlines the high degree of structural versatility that the globin fold is capable of, enabling it to perform a diversity of functions.

PubMed: 26094577
DOI: 10.1038/srep11407

実験手法

X-RAY DIFFRACTION (1.65 Å)