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Mechanism of Rab1b deactivation by the Legionella pneumophila GAP LepB

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Mechanism of Rab1b deactivation by the Legionella pneumophila GAP LepB. / Mihai Gazdag, Emerich; Streller, Alexandra; Haneburger, Ina; Hilbi, Hubert; Vetter, Ingrid R; Goody, Roger S; Itzen, Aymelt.

in: EMBO REP, Jahrgang 14, Nr. 2, 02.2013, S. 199-205.

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

Harvard

Mihai Gazdag, E, Streller, A, Haneburger, I, Hilbi, H, Vetter, IR, Goody, RS & Itzen, A 2013, 'Mechanism of Rab1b deactivation by the Legionella pneumophila GAP LepB', EMBO REP, Jg. 14, Nr. 2, S. 199-205. https://doi.org/10.1038/embor.2012.211

APA

Mihai Gazdag, E., Streller, A., Haneburger, I., Hilbi, H., Vetter, I. R., Goody, R. S., & Itzen, A. (2013). Mechanism of Rab1b deactivation by the Legionella pneumophila GAP LepB. EMBO REP, 14(2), 199-205. https://doi.org/10.1038/embor.2012.211

Vancouver

Mihai Gazdag E, Streller A, Haneburger I, Hilbi H, Vetter IR, Goody RS et al. Mechanism of Rab1b deactivation by the Legionella pneumophila GAP LepB. EMBO REP. 2013 Feb;14(2):199-205. https://doi.org/10.1038/embor.2012.211

Bibtex

@article{0ceb8c3296aa4a7ebe094cb18ee5102c,
title = "Mechanism of Rab1b deactivation by the Legionella pneumophila GAP LepB",
abstract = "Legionella pneumophila is an intracellularly surviving pathogen that releases about 270 different proteins into the host cell during infection. A set of secreted proteins takes control of the vesicular trafficking regulator Rab1. Legionella LepB inactivates Rab1 by acting as a GTPase-activating protein (GAP). We present the crystal structure of the Rab1b:LepB complex together with a thorough biochemical analysis and show that the GAP domain of LepB consists of an unusual fold. LepB acts by an atypical RabGAP mechanism that is reminiscent of classical GAPs and therefore sets the protein apart from mammalian TBC-like GAPs. Surprisingly, LepB can function as a GAP for Rab3, Rab8, Rab13 and Rab35, too, suggesting that it has a broader cellular role than previously thought.",
keywords = "Amino Acid Sequence, Amino Acid Substitution, Bacterial Proteins, Conserved Sequence, Crystallography, X-Ray, Guanosine Triphosphate, Host-Pathogen Interactions, Humans, Hydrolysis, Legionella pneumophila, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Structure, Quaternary, Protein Structure, Secondary, Protein Structure, Tertiary, rab GTP-Binding Proteins, rab1 GTP-Binding Proteins, Journal Article, Research Support, Non-U.S. Gov't",
author = "{Mihai Gazdag}, Emerich and Alexandra Streller and Ina Haneburger and Hubert Hilbi and Vetter, {Ingrid R} and Goody, {Roger S} and Aymelt Itzen",
year = "2013",
month = feb,
doi = "10.1038/embor.2012.211",
language = "English",
volume = "14",
pages = "199--205",
journal = "EMBO REP",
issn = "1469-221X",
publisher = "NATURE PUBLISHING GROUP",
number = "2",

}

RIS

TY - JOUR

T1 - Mechanism of Rab1b deactivation by the Legionella pneumophila GAP LepB

AU - Mihai Gazdag, Emerich

AU - Streller, Alexandra

AU - Haneburger, Ina

AU - Hilbi, Hubert

AU - Vetter, Ingrid R

AU - Goody, Roger S

AU - Itzen, Aymelt

PY - 2013/2

Y1 - 2013/2

N2 - Legionella pneumophila is an intracellularly surviving pathogen that releases about 270 different proteins into the host cell during infection. A set of secreted proteins takes control of the vesicular trafficking regulator Rab1. Legionella LepB inactivates Rab1 by acting as a GTPase-activating protein (GAP). We present the crystal structure of the Rab1b:LepB complex together with a thorough biochemical analysis and show that the GAP domain of LepB consists of an unusual fold. LepB acts by an atypical RabGAP mechanism that is reminiscent of classical GAPs and therefore sets the protein apart from mammalian TBC-like GAPs. Surprisingly, LepB can function as a GAP for Rab3, Rab8, Rab13 and Rab35, too, suggesting that it has a broader cellular role than previously thought.

AB - Legionella pneumophila is an intracellularly surviving pathogen that releases about 270 different proteins into the host cell during infection. A set of secreted proteins takes control of the vesicular trafficking regulator Rab1. Legionella LepB inactivates Rab1 by acting as a GTPase-activating protein (GAP). We present the crystal structure of the Rab1b:LepB complex together with a thorough biochemical analysis and show that the GAP domain of LepB consists of an unusual fold. LepB acts by an atypical RabGAP mechanism that is reminiscent of classical GAPs and therefore sets the protein apart from mammalian TBC-like GAPs. Surprisingly, LepB can function as a GAP for Rab3, Rab8, Rab13 and Rab35, too, suggesting that it has a broader cellular role than previously thought.

KW - Amino Acid Sequence

KW - Amino Acid Substitution

KW - Bacterial Proteins

KW - Conserved Sequence

KW - Crystallography, X-Ray

KW - Guanosine Triphosphate

KW - Host-Pathogen Interactions

KW - Humans

KW - Hydrolysis

KW - Legionella pneumophila

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Protein Binding

KW - Protein Structure, Quaternary

KW - Protein Structure, Secondary

KW - Protein Structure, Tertiary

KW - rab GTP-Binding Proteins

KW - rab1 GTP-Binding Proteins

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1038/embor.2012.211

DO - 10.1038/embor.2012.211

M3 - SCORING: Journal article

C2 - 23288104

VL - 14

SP - 199

EP - 205

JO - EMBO REP

JF - EMBO REP

SN - 1469-221X

IS - 2

ER -