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pubmed-article:20454456pubmed:abstractTextThe ABC transporter OpuA from Lactococcus lactis transports glycine betaine upon activation by threshold values of ionic strength. In this study, the ligand binding characteristics of purified OpuA in a detergent-solubilized state and of its substrate-binding domain produced as soluble protein (OpuAC) was characterized.lld:pubmed
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pubmed-article:20454456pubmed:articleTitleLigand binding and crystal structures of the substrate-binding domain of the ABC transporter OpuA.lld:pubmed
pubmed-article:20454456pubmed:affiliationBiochemistry Department, Groningen Biomolecular Sciences and Biotechnology Institute, Netherlands Proteomics Centre, University of Groningen, Groningen, The Netherlands.lld:pubmed
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