3TFG

Crystal structure of an H-NOX protein from Nostoc sp. PCC 7120, L66W/L67W double mutant

Summary for 3TFG

• Entry DOI: 10.2210/pdb3tfg/pdb
• Related: 2O09 2O0C 2O0G 3TF0 3TF1 3TF8 3TF9 3TFA 3TFD 3TFE 3TFF 3TFG
• Descriptor: Alr2278 protein, PROTOPORPHYRIN IX CONTAINING FE, MALONIC ACID, ... (4 entities in total)
• Functional Keywords: heme-based sensor domain, gas binding, signaling protein
• Biological source: Nostoc sp. PCC 7120
• Total number of polymer chains: 2
• Total formula weight: 44160.59

Authors

Winter, M.B.,Herzik Jr., M.A.,Kuriyan, J.,Marletta, M.A. (deposition date: 2011-08-15, release date: 2011-11-09, Last modification date: 2023-09-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.9003 Å)