3TF0

Crystal structure of an H-NOX protein from T. tengcongensis

3TF0 の概要

• エントリーDOI: 10.2210/pdb3tf0/pdb
• 関連するPDBエントリー: 1U4H 1U55 1U56 3TF1 3TF8 3TF9 3TFA 3TFD 3TFE 3TFF 3TFG
• 分子名称: Methyl-accepting chemotaxis protein, PROTOPORPHYRIN IX CONTAINING FE, OXYGEN MOLECULE, ... (5 entities in total)
• 機能のキーワード: heme-based methyl-accepting chemotaxis protein, gas binding, signaling protein
• 由来する生物種: Caldanaerobacter subterraneus subsp. tengcongensis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 45451.02

構造登録者

Winter, M.B.,Herzik Jr., M.A.,Kuriyan, J.,Marletta, M.A. (登録日: 2011-08-15, 公開日: 2011-11-09, 最終更新日: 2023-09-13)

主引用文献

Winter, M.B.,Herzik, M.A.,Kuriyan, J.,Marletta, M.A.
Tunnels modulate ligand flux in a heme nitric oxide/oxygen binding (H-NOX) domain.
Proc.Natl.Acad.Sci.USA, 108:E881-E889, 2011

PubMed Abstract: Interior topological features, such as pockets and channels, have evolved in proteins to regulate biological functions by facilitating the diffusion of biomolecules. Decades of research using the globins as model heme proteins have clearly highlighted the importance of gas pockets around the heme in controlling the capture and release of O(2). However, much less is known about how ligand migration contributes to the diverse functions of other heme protein scaffolds. Heme nitric oxide/oxygen binding (H-NOX) domains are a conserved family of gas-sensing heme proteins with a divergent fold that are critical to numerous signaling pathways. Utilizing X-ray crystallography with xenon, a tunnel network has been shown to serve as a molecular pathway for ligand diffusion. Structure-guided mutagenesis results show that the tunnels have unexpected effects on gas-sensing properties in H-NOX domains. The findings provide insights on how the flux of biomolecules through protein scaffolds modulates protein chemistry.

PubMed: 21997213
DOI: 10.1073/pnas.1114038108

実験手法

X-RAY DIFFRACTION (1.743 Å)