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

Department of Life Sciences

University of York

Research output: Contribution to journal › Article › peer-review

25 Citations (SciVal)

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
Early online date	5 Sept 2015
DOIs	https://doi.org/10.1074/jbc.M115.656603
Publication status	Published - Nov 2015

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10.1074/jbc.M115.656603

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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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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

Y1 - 2015/11

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.

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UR - http://dx.doi.org/10.1074/jbc.M115.656603

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DO - 10.1074/jbc.M115.656603

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SP - 27113

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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

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Andrew Watts

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

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