Publication

Functional Diversity of Tandem Substrate-Binding Domains in ABC Transporters from Pathogenic Bacteria

Fulyani, F., Schuurman-Wolters, G. K., Vujicic - Zagar, A., Guskov, A., Slotboom, D-J. & Poolman, B., 8-Oct-2013, In : Structure. 21, 10, p. 1879-1888 10 p.

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DOI

The ATP-binding cassette (ABC) transporter GInPQ is an essential uptake system for amino acids in gram-positive pathogens and related nonpathogenic bacteria. The transporter has tandem substrate-binding domains (SBDs) fused to each transmembrane domain, giving rise to four SBDs per functional transporter complex. We have determined the crystal structures and ligand-binding properties of the SBDs of GInPQ from Enterococcus faecalis, Streptococcus pneumoniae, and Lactococcus lactis. The tandem SBDs differ in substrate specificity and affinity, allowing cells to efficiently accumulate different amino acids via a single ABC transporter. The combined structural, functional, and thermodynamic analysis revealed the roles of individual residues in determining the substrate affinity. We succeeded in converting a low-affinity SBD into a high-affinity receptor and vice versa. Our data indicate that a small number of residues that reside in the binding pocket constitute the major affinity determinants of the SBDs.

Original languageEnglish
Pages (from-to)1879-1888
Number of pages10
JournalStructure
Volume21
Issue number10
Publication statusPublished - 8-Oct-2013

    Keywords

  • ESCHERICHIA-COLI, CASSETTE TRANSPORTER, MALTOSE TRANSPORTER, CRYSTAL-STRUCTURE, BTUCD-F, PROTEIN, ATP, GLUTAMINE, IMPORTER, COMPLEX

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