An Investigation of the Ligand-Binding Site of the Glutamine-Binding Protein of Escherichia coli Using Rotational-Echo Double-Resonance NMR

Biochemistry ◽  
1994 ◽  
Vol 33 (29) ◽  
pp. 8651-8661 ◽  
Author(s):  
Andrew W. Hing ◽  
Nico Tjandra ◽  
Patricia F. Cottam ◽  
Jacob Schaefer ◽  
Chien Ho
2011 ◽  
Vol 11 (1) ◽  
pp. 64 ◽  
Author(s):  
Tiina A Riihimäki ◽  
Soili Hiltunen ◽  
Martina Rangl ◽  
Henri R Nordlund ◽  
Juha AE Määttä ◽  
...  

2009 ◽  
Vol 390 (11) ◽  
Author(s):  
Christine Oswald ◽  
Sander H.J. Smits ◽  
Marina Höing ◽  
Erhard Bremer ◽  
Lutz Schmitt

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.


Biochemistry ◽  
2018 ◽  
Vol 57 (11) ◽  
pp. 1758-1766
Author(s):  
S. A. Adediran ◽  
Kumar Subarno Sarkar ◽  
R. F. Pratt

1999 ◽  
Vol 274 (52) ◽  
pp. 37210-37218 ◽  
Author(s):  
Z. Galen Wo ◽  
Kamaldeep K. Chohan ◽  
Haiying Chen ◽  
Michael J. Sutcliffe ◽  
Robert E. Oswald

2002 ◽  
Vol 76 (6) ◽  
pp. 606 ◽  
Author(s):  
Takahiro Hirano ◽  
In Taek Lim ◽  
Don Moon Kim ◽  
Xiang-Guo Zheng ◽  
Kazuo Yoshihara ◽  
...  

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