The 91 kDa oligomeric ring-shaped ligand binding protein TRAP ( trp RNA binding attenuation protein) regulates the expression of a series of genes involved in tryptophan (Trp) biosynthesis in bacilli. When cellular Trp levels rise, the free amino acid binds to sites buried in the interfaces between each of the 11 (or 12, depending on the species) protomers in the ring. Crystal structures of Trp-bound TRAP show the Trp ligands are sequestered from solvent by a pair of loops from adjacent...
[NMR paper] Chemical Conformation of the Essential Glutamate Site of the c-Ring within Thermophilic Bacillus FoF1-ATP Synthase Determined by Solid-State NMR Based on its Isolated c-Ring Structure
Chemical Conformation of the Essential Glutamate Site of the c-Ring within Thermophilic Bacillus FoF1-ATP Synthase Determined by Solid-State NMR Based on its Isolated c-Ring Structure
Proton translocation through the membrane-embedded F(o) component of F-type ATP synthase (F(o)F(1)) is facilitated by the rotation of the F(o) c-subunit ring (c-ring), carrying protons at essential acidic amino acid residues. Cryo-electron microscopy (Cryo-EM) structures of F(o)F(1) suggest a unique proton translocation mechanism. To elucidate it based on the chemical conformation of the essential acidic...
[NMR paper] Direct assignment of 13C solid-state NMR signals of TFoF1 ATP synthase subunit c-ring in lipid membranes and its implication for the ring structure.
Direct assignment of 13C solid-state NMR signals of TFoF1 ATP synthase subunit c-ring in lipid membranes and its implication for the ring structure.
Direct assignment of 13C solid-state NMR signals of TFoF1 ATP synthase subunit c-ring in lipid membranes and its implication for the ring structure.
J Biomol NMR. 2017 Dec 02;:
Authors: Kang SJ, Todokoro Y, Bak S, Suzuki T, Yoshida M, Fujiwara T, Akutsu H
Abstract
FoF1-ATP synthase catalyzes ATP hydrolysis/synthesis coupled with a transmembrane H+ translocation in membranes. The Fo...
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Direct assignment of 13 C solid-state NMR signals of TF o F 1 ATP synthase subunit c -ring in lipid membranes and its implication for the ring structure
Direct assignment of 13 C solid-state NMR signals of TF o F 1 ATP synthase subunit c -ring in lipid membranes and its implication for the ring structure
Abstract
FoF1-ATP synthase catalyzes ATP hydrolysis/synthesis coupled with a transmembrane H+ translocation in membranes. The Fo c-subunit ring plays a major role in this reaction. We have developed an assignment strategy for solid-state 13C NMR (ssNMR) signals of the Fo c-subunit ring of thermophilic Bacillus PS3 (TFo ...
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[NMR paper] Label-free quantitative 1H NMR spectroscopy to study low-affinity ligand-protein interactions in solution: A contribution to the mechanism of polyphenol-mediated astringency.
Label-free quantitative 1H NMR spectroscopy to study low-affinity ligand-protein interactions in solution: A contribution to the mechanism of polyphenol-mediated astringency.
Label-free quantitative 1H NMR spectroscopy to study low-affinity ligand-protein interactions in solution: A contribution to the mechanism of polyphenol-mediated astringency.
PLoS One. 2017;12(9):e0184487
Authors: Delius J, Frank O, Hofmann T
Abstract
Nuclear magnetic resonance (NMR) spectroscopy is well-established in assessing the binding affinity between...
[NMR paper] G-protein-coupled receptor structure, ligand binding and activation as studied by solid-state NMR spectroscopy.
G-protein-coupled receptor structure, ligand binding and activation as studied by solid-state NMR spectroscopy.
G-protein-coupled receptor structure, ligand binding and activation as studied by solid-state NMR spectroscopy.
Biochem J. 2013 Mar 15;450(3):443-57
Authors: Ding X, Zhao X, Watts A
Abstract
GPCRs (G-protein-coupled receptors) are versatile signalling molecules at the cell surface and make up the largest and most diverse family of membrane receptors in the human genome. They convert a large variety of extracellular stimuli into...
Insights into Ligand-Mediated Activation of an Oligomeric Ring-Shaped Gene-Regulatory Protein from Solution- and Solid-State NMR
Linear Mode
