Literature summary for 7.6.2.9 extracted from

Pittelkow, M.; Tschapek, B.; Smits, S.H.; Schmitt, L.; Bremer, E.
The crystal structure of the substrate-binding protein OpuBC from Bacillus subtilis in complex with choline (2011), J. Mol. Biol., 411, 53-67.

Crystallization (Commentary)

Crystallization (Comment)	Organism
substrate-binding protein OpuBC in complex with choline, to 1.6 A resolution. The positively charged trimethylammonium head group of choline is wedged into an aromatic cage formed by four tyrosine residues and is bound via cation-pi interactions. The hydroxyl group of choline protrudes out of this aromatic cage and makes a single interaction with residue Gln19. A water network stabilizes choline within its substrate-binding site and promotes indirect interactions between the two lobes of the OpuBC protein. Disruption of this intricate water network strongly reduces choline binding affinity or abrogates ligand binding	Bacillus subtilis

Crystallization (Comment)

Organism

substrate-binding protein OpuBC in complex with choline, to 1.6 A resolution. The positively charged trimethylammonium head group of choline is wedged into an aromatic cage formed by four tyrosine residues and is bound via cation-pi interactions. The hydroxyl group of choline protrudes out of this aromatic cage and makes a single interaction with residue Gln19. A water network stabilizes choline within its substrate-binding site and promotes indirect interactions between the two lobes of the OpuBC protein. Disruption of this intricate water network strongly reduces choline binding affinity or abrogates ligand binding

Bacillus subtilis

Protein Variants

Protein Variants	Comment	Organism
D149A	decrease in choline binding affinity by approximately 18fold	Bacillus subtilis
D149A/L155A	decrease in choline binding affinity by approximately 38fold	Bacillus subtilis
D74A	mutant is unable to bind choline	Bacillus subtilis
L155A	decrease in choline binding affinity by approximately 25fold	Bacillus subtilis
M21A	decrease in choline binding affinity by approximately 3fold	Bacillus subtilis
N115A	mutant is unable to bind choline	Bacillus subtilis
Q19A	decrease in choline binding affinity by approximately 15fold	Bacillus subtilis
Q19A/L155A	mutant is unable to bind choline	Bacillus subtilis

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	Q45462	choline-binding protein	-
Bacillus subtilis JH642	Q45462	choline-binding protein	-

Synonyms

Synonyms	Comment	Organism
OpuBC	-	Bacillus subtilis