3tfg

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

spinqualitylabelsall models 3tfg, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3tfg is a 2 chain structure with sequence from Nostoc sp. PCC 7120 = FACHB-418. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9003Å Ligands: HEM, MLA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8YUQ7_NOSS1 Publication Abstract from PubMed 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. Tunnels modulate ligand flux in a heme nitric oxide/oxygen binding (H-NOX) domain.,Winter MB, Herzik MA Jr, Kuriyan J, Marletta MA Proc Natl Acad Sci U S A. 2011 Oct 25;108(43):E881-9. Epub 2011 Oct 12. PMID:21997213 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA