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

doi:10.1074/jbc.M115.656603

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 journal › Article › peer-review

Abstract

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 language	English
Pages (from-to)	27113-27123
Number of pages	11
Journal	Journal of Biological Chemistry
Volume	290
Issue number	45
DOIs	https://doi.org/10.1074/jbc.M115.656603
Publication status	Published - 6 Nov 2015

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

abstract = "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.",

author = "Marcus Fischer and Hopkins, {Adam P.} and Emmanuele Severi and Judith Hawkhead and Daniel Bawdon and Watts, {Andrew G.} and Hubbard, {Roderick E.} and Thomas, {Gavin H.}",

year = "2015",

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doi = "10.1074/jbc.M115.656603",

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T1 - Tripartite ATP-independent Periplasmic (TRAP) Transporters use an arginine-mediated selectivity filter for high affinity substrate binding

AU - Fischer, Marcus

AU - Hopkins, Adam P.

AU - Severi, Emmanuele

AU - Hawkhead, Judith

AU - Bawdon, Daniel

AU - Watts, Andrew G.

AU - Hubbard, Roderick E.

AU - Thomas, Gavin H.

PY - 2015/11/6

Y1 - 2015/11/6

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84946779763&partnerID=8YFLogxK

U2 - 10.1074/jbc.M115.656603

DO - 10.1074/jbc.M115.656603

M3 - Article

AN - SCOPUS:84946779763

SN - 0021-9258

VL - 290

SP - 27113

EP - 27123

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 45

ER -

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

Abstract

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