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High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA

Standard

High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA. / Schoebel, Stefan; Blankenfeldt, Wulf; Goody, Roger S; Itzen, Aymelt.

in: EMBO REP, Jahrgang 11, Nr. 8, 08.2010, S. 598-604.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Schoebel, S, Blankenfeldt, W, Goody, RS & Itzen, A 2010, 'High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA', EMBO REP, Jg. 11, Nr. 8, S. 598-604. https://doi.org/10.1038/embor.2010.97

APA

Schoebel, S., Blankenfeldt, W., Goody, R. S., & Itzen, A. (2010). High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA. EMBO REP, 11(8), 598-604. https://doi.org/10.1038/embor.2010.97

Vancouver

Schoebel S, Blankenfeldt W, Goody RS, Itzen A. High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA. EMBO REP. 2010 Aug;11(8):598-604. https://doi.org/10.1038/embor.2010.97

Bibtex

@article{d1a484e02a7a4f45ad395e8c7456d19a,
title = "High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA",
abstract = "The DrrA protein of Legionella pneumophila is involved in mistargeting of endoplasmic reticulum-derived vesicles to Legionella-containing vacuoles through recruitment of the small GTPase Rab1. To this effect, DrrA binds specifically to phosphatidylinositol 4-phosphate (PtdIns(4)P) lipids on the cytosolic surface of the phagosomal membrane shortly after infection. In this study, we present the atomic structure of the PtdIns(4)P-binding domain of a protein (DrrA) from a human pathogen. A detailed kinetic investigation of its interaction with PtdIns(4)P reveals that DrrA binds to this phospholipid with, as yet unprecedented, high affinity, suggesting that DrrA can sense a very low abundance of the lipid.",
keywords = "Bacterial Proteins, Binding Sites, Crystallography, X-Ray, Guanine Nucleotide Exchange Factors, Humans, Legionella pneumophila, Models, Molecular, Molecular Sequence Data, Phagocytosis, Phosphatidylinositol Phosphates, Protein Binding, Protein Conformation, Protein Interaction Domains and Motifs, rab1 GTP-Binding Proteins, Journal Article",
author = "Stefan Schoebel and Wulf Blankenfeldt and Goody, {Roger S} and Aymelt Itzen",
year = "2010",
month = aug,
doi = "10.1038/embor.2010.97",
language = "English",
volume = "11",
pages = "598--604",
journal = "EMBO REP",
issn = "1469-221X",
publisher = "NATURE PUBLISHING GROUP",
number = "8",

}

RIS

TY - JOUR

T1 - High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA

AU - Schoebel, Stefan

AU - Blankenfeldt, Wulf

AU - Goody, Roger S

AU - Itzen, Aymelt

PY - 2010/8

Y1 - 2010/8

N2 - The DrrA protein of Legionella pneumophila is involved in mistargeting of endoplasmic reticulum-derived vesicles to Legionella-containing vacuoles through recruitment of the small GTPase Rab1. To this effect, DrrA binds specifically to phosphatidylinositol 4-phosphate (PtdIns(4)P) lipids on the cytosolic surface of the phagosomal membrane shortly after infection. In this study, we present the atomic structure of the PtdIns(4)P-binding domain of a protein (DrrA) from a human pathogen. A detailed kinetic investigation of its interaction with PtdIns(4)P reveals that DrrA binds to this phospholipid with, as yet unprecedented, high affinity, suggesting that DrrA can sense a very low abundance of the lipid.

AB - The DrrA protein of Legionella pneumophila is involved in mistargeting of endoplasmic reticulum-derived vesicles to Legionella-containing vacuoles through recruitment of the small GTPase Rab1. To this effect, DrrA binds specifically to phosphatidylinositol 4-phosphate (PtdIns(4)P) lipids on the cytosolic surface of the phagosomal membrane shortly after infection. In this study, we present the atomic structure of the PtdIns(4)P-binding domain of a protein (DrrA) from a human pathogen. A detailed kinetic investigation of its interaction with PtdIns(4)P reveals that DrrA binds to this phospholipid with, as yet unprecedented, high affinity, suggesting that DrrA can sense a very low abundance of the lipid.

KW - Bacterial Proteins

KW - Binding Sites

KW - Crystallography, X-Ray

KW - Guanine Nucleotide Exchange Factors

KW - Humans

KW - Legionella pneumophila

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Phagocytosis

KW - Phosphatidylinositol Phosphates

KW - Protein Binding

KW - Protein Conformation

KW - Protein Interaction Domains and Motifs

KW - rab1 GTP-Binding Proteins

KW - Journal Article

U2 - 10.1038/embor.2010.97

DO - 10.1038/embor.2010.97

M3 - SCORING: Journal article

C2 - 20616805

VL - 11

SP - 598

EP - 604

JO - EMBO REP

JF - EMBO REP

SN - 1469-221X

IS - 8

ER -