scholarly journals The Crystal Structure of a Cockroach Pheromone-binding Protein Suggests a New Ligand Binding and Release Mechanism

2003 ◽  
Vol 278 (32) ◽  
pp. 30213-30218 ◽  
Author(s):  
Audrey Lartigue ◽  
Arnaud Gruez ◽  
Silvia Spinelli ◽  
Stéphane Rivière ◽  
Rémy Brossut ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Ligand Binding ◽  
Binding Protein ◽  
Release Mechanism ◽  
Pheromone Binding Protein

Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors

Nature ◽  
2001 ◽  
Vol 411 (6835) ◽  
pp. 269-276 ◽  
Author(s):  
KatjuS̆a Brejc ◽  
Willem J. van Dijk ◽  
Remco V. Klaassen ◽  
Mascha Schuurmans ◽  
John van der Oost ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Ligand Binding ◽  
Nicotinic Receptors ◽  
Binding Protein ◽  
Binding Domain ◽  
Ligand Binding Domain

scholarly journals Functional clues from the crystal structure of an orphan periplasmic ligand-binding protein fromTreponema pallidum

2017 ◽  
Vol 26 (4) ◽  
pp. 847-856 ◽  
Author(s):  
Chad. A. Brautigam ◽  
Ranjit K. Deka ◽  
Wei Z. Liu ◽  
Diana R. Tomchick ◽  
Michael V. Norgard
Keyword(s):  
Crystal Structure ◽  
Ligand Binding ◽  
Binding Protein

Structural analysis of the choline-binding protein ChoX in a semi-closed and ligand-free conformation

2009 ◽  
Vol 390 (11) ◽  
Author(s):  
Christine Oswald ◽  
Sander H.J. Smits ◽  
Marina Höing ◽  
Erhard Bremer ◽  
Lutz Schmitt
Keyword(s):  
Crystal Structure ◽  
Structural Analysis ◽  
Ligand Binding ◽  
Closed Form ◽  
Binding Site ◽  
Sinorhizobium Meliloti ◽  
Binding Protein ◽  
Ligand Binding Site ◽  
Abc Transport ◽  
Ligand Free

Abstract The periplasmic ligand-binding protein ChoX is part of the ABC transport system ChoVWX that imports choline as a nutrient into the soil bacterium Sinorhizobium meliloti. We have recently reported the crystal structures of ChoX in complex with its ligands choline and acetylcholine and the structure of a fully closed but substrate-free state of ChoX. This latter structure revealed an architecture of the ligand-binding site that is superimposable to the closed, ligand-bound form of ChoX. We report here the crystal structure of ChoX in an unusual, ligand-free conformation that represents a semi-closed form of ChoX. The analysis revealed a subdomain movement in the N-lobe of ChoX. Comparison with the two well-characterized substrate binding proteins, MBP and HisJ, suggests the presence of a similar subdomain in these proteins.

scholarly journals Ligand Binding Turns Moth Pheromone-binding Protein into a pH Sensor

2009 ◽  
Vol 284 (46) ◽  
pp. 32167-32177 ◽  
Author(s):  
Uma V. Katre ◽  
Suman Mazumder ◽  
Rabi K. Prusti ◽  
Smita Mohanty
Keyword(s):  
Ligand Binding ◽  
Binding Protein ◽  
Ph Sensor ◽  
Pheromone Binding Protein

scholarly journals Sulfur Single-wavelength Anomalous Diffraction Crystal Structure of a Pheromone-Binding Protein from the HoneybeeApis melliferaL

2003 ◽  
Vol 279 (6) ◽  
pp. 4459-4464 ◽  
Author(s):  
Audrey Lartigue ◽  
Arnaud Gruez ◽  
Loïc Briand ◽  
Florence Blon ◽  
Valérie Bézirard ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Binding Protein ◽  
Anomalous Diffraction ◽  
Pheromone Binding Protein
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