3TF1
Crystal structure of an H-NOX protein from T. tengcongensis under 6 atm of xenon
Summary for 3TF1
| Entry DOI | 10.2210/pdb3tf1/pdb |
| Related | 1U4H 1U55 1U56 3TF0 3TF8 3TF9 3TFA 3TFD 3TFE 3TFF 3TFG |
| Descriptor | Methyl-accepting chemotaxis protein, PROTOPORPHYRIN IX CONTAINING FE, OXYGEN MOLECULE, ... (6 entities in total) |
| Functional Keywords | heme-based methyl-accepting chemotaxis protein, gas binding, signaling protein |
| Biological source | Caldanaerobacter subterraneus subsp. tengcongensis |
| Total number of polymer chains | 2 |
| Total formula weight | 45976.19 |
| 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 Cited by 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: 21997213DOI: 10.1073/pnas.1114038108 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.0369 Å) |
Structure validation
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