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

Research output: Contribution to journalArticle

10 Citations (Scopus)

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 languageEnglish
Pages (from-to)27113-27123
Number of pages11
JournalJournal of Biological Chemistry
Volume290
Issue number45
Early online date5 Sep 2015
DOIs
Publication statusPublished - Nov 2015

Fingerprint

Arginine
Adenosine Triphosphate
Carrier Proteins
Substrates
Haemophilus influenzae
N-Acetylneuraminic Acid
Virulence

Cite this

Tripartite ATP-independent Periplasmic (TRAP) Transporters use an arginine-mediated selectivity filter for high affinity substrate binding. / Fischer, Marcus; Hopkins, Adam P.; Severi, Emmanuele; Hawkhead, Judith; Bawdon, Daniel; Watts, Andrew G.; Hubbard, Roderick E.; Thomas, Gavin H.

In: Journal of Biological Chemistry, Vol. 290, No. 45, 11.2015, p. 27113-27123.

Research output: Contribution to journalArticle

Fischer, Marcus ; Hopkins, Adam P. ; Severi, Emmanuele ; Hawkhead, Judith ; Bawdon, Daniel ; Watts, Andrew G. ; Hubbard, Roderick E. ; Thomas, Gavin H. / Tripartite ATP-independent Periplasmic (TRAP) Transporters use an arginine-mediated selectivity filter for high affinity substrate binding. In: Journal of Biological Chemistry. 2015 ; Vol. 290, No. 45. pp. 27113-27123.
@article{4d7823cb9345441b911806297c22aa30,
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",
month = "11",
doi = "10.1074/jbc.M115.656603",
language = "English",
volume = "290",
pages = "27113--27123",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "45",

}

TY - JOUR

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.

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

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

U2 - 10.1074/jbc.M115.656603

DO - 10.1074/jbc.M115.656603

M3 - Article

VL - 290

SP - 27113

EP - 27123

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 45

ER -