Tripartite ATP-independent Periplasmic (TRAP) Transporters use an arginine-mediated selectivity filter for high affinity substrate binding

Marcus Fischer, Adam P. Hopkins, Emmanuele Severi, Judith Hawkhead, Daniel Bawdon, Andrew G. Watts, Roderick E. Hubbard, Gavin H. Thomas*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Background: Haemophilus influenzae requires a substrate-binding protein (SBP)-dependent TRAP transporter to acquire sialic acid. Results: A conserved arginine residue in the SBP is essential for the high affinity and carboxylate specificity of the TRAP transporter. Conclusion: The arginine/carboxylate interaction in TRAP SBPs restricts substrate range to carboxylate-containing substrates. Significance: The study reveals the mechanism by which a key bimolecular interaction underpins bacterial virulence.

Original languageEnglish
Pages (from-to)27113-27123
Number of pages11
JournalJournal of Biological Chemistry
Issue number45
Publication statusPublished - 6 Nov 2015

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