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Literature summary for 7.6.2.9 extracted from

  • Du, Y.; Shi, W.W.; He, Y.X.; Yang, Y.H.; Zhou, C.Z.; Chen, Y.
    Structures of the substrate-binding protein provide insights into the multiple compatible solute binding specificities of the Bacillus subtilis ABC transporter OpuC (2011), Biochem. J., 436, 283-289.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment) Organism
substrate-binding protein OpuCC in the apo-form and in complex with carnitine, glycine betaine, choline and ectoine to 2.3, 2.7, 2.4, 1.9 and 2.1 A resolution, respectively. OpuCC is composed of two alpha/beta/alpha globular sandwich domains linked by two hinge regions, with a substrate-binding pocket located at the interdomain cleft. Upon substrate binding, the two domains shift towards each other to trap the substrate Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
T94D shares a quite similar pattern of fluorescence spectrum to that of the paralogue OpuBC. Only choline can trigger obvious changes of fluorescence intensity of mutant T94D, whereas carnitine, GB and ectoine cannot Bacillus subtilis
Y91A complete loss of binding affinity Bacillus subtilis
Y91F slight decrease in binding affinity Bacillus subtilis
Y91W slight decrease in binding affinity Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis O32243
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Synonyms

Synonyms Comment Organism
glycine betaine/carnitine/choline-binding protein
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Bacillus subtilis
OpuCC
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Bacillus subtilis