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Adenylylation of Tyr77 stabilizes Rab1b GTPase in an active state

Standard

Adenylylation of Tyr77 stabilizes Rab1b GTPase in an active state : A molecular dynamics simulation analysis. / Luitz, Manuel P; Bomblies, Rainer; Ramcke, Evelyn; Itzen, Aymelt; Zacharias, Martin.

In: SCI REP-UK, Vol. 6, 28.01.2016, p. 19896.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Luitz, MP, Bomblies, R, Ramcke, E, Itzen, A & Zacharias, M 2016, 'Adenylylation of Tyr77 stabilizes Rab1b GTPase in an active state: A molecular dynamics simulation analysis', SCI REP-UK, vol. 6, pp. 19896. https://doi.org/10.1038/srep19896

APA

Luitz, M. P., Bomblies, R., Ramcke, E., Itzen, A., & Zacharias, M. (2016). Adenylylation of Tyr77 stabilizes Rab1b GTPase in an active state: A molecular dynamics simulation analysis. SCI REP-UK, 6, 19896. https://doi.org/10.1038/srep19896

Vancouver

Luitz MP, Bomblies R, Ramcke E, Itzen A, Zacharias M. Adenylylation of Tyr77 stabilizes Rab1b GTPase in an active state: A molecular dynamics simulation analysis. SCI REP-UK. 2016 Jan 28;6:19896. https://doi.org/10.1038/srep19896

Bibtex

@article{87737e5a746347d386fe464283be4908,
title = "Adenylylation of Tyr77 stabilizes Rab1b GTPase in an active state: A molecular dynamics simulation analysis",
abstract = "The pathogenic pathway of Legionella pneumophila exploits the intercellular vesicle transport system via the posttranslational attachment of adenosine monophosphate (AMP) to the Tyr77 sidechain of human Ras like GTPase Rab1b. The modification, termed adenylylation, is performed by the bacterial enzyme DrrA/SidM, however the effect on conformational properties of the molecular switch mechanism of Rab1b remained unresolved. In this study we find that the adenylylation of Tyr77 stabilizes the active Rab1b state by locking the switch in the active signaling conformation independent of bound GTP or GDP and that electrostatic interactions due to the additional negative charge in the switch region make significant contributions. The stacking interaction between adenine and Phe45 however, seems to have only minor influence on this stabilisation. The results may also have implications for the mechanistic understanding of conformational switching in other signaling proteins. ",
keywords = "Adenosine Monophosphate, Guanosine Triphosphate, Molecular Dynamics Simulation, Protein Binding, Protein Conformation, Protein Stability, Static Electricity, Tyrosine, rab1 GTP-Binding Proteins, Journal Article, Research Support, Non-U.S. Gov't",
author = "Luitz, {Manuel P} and Rainer Bomblies and Evelyn Ramcke and Aymelt Itzen and Martin Zacharias",
year = "2016",
month = jan,
day = "28",
doi = "10.1038/srep19896",
language = "English",
volume = "6",
pages = "19896",
journal = "SCI REP-UK",
issn = "2045-2322",
publisher = "NATURE PUBLISHING GROUP",

}

RIS

TY - JOUR

T1 - Adenylylation of Tyr77 stabilizes Rab1b GTPase in an active state

T2 - A molecular dynamics simulation analysis

AU - Luitz, Manuel P

AU - Bomblies, Rainer

AU - Ramcke, Evelyn

AU - Itzen, Aymelt

AU - Zacharias, Martin

PY - 2016/1/28

Y1 - 2016/1/28

N2 - The pathogenic pathway of Legionella pneumophila exploits the intercellular vesicle transport system via the posttranslational attachment of adenosine monophosphate (AMP) to the Tyr77 sidechain of human Ras like GTPase Rab1b. The modification, termed adenylylation, is performed by the bacterial enzyme DrrA/SidM, however the effect on conformational properties of the molecular switch mechanism of Rab1b remained unresolved. In this study we find that the adenylylation of Tyr77 stabilizes the active Rab1b state by locking the switch in the active signaling conformation independent of bound GTP or GDP and that electrostatic interactions due to the additional negative charge in the switch region make significant contributions. The stacking interaction between adenine and Phe45 however, seems to have only minor influence on this stabilisation. The results may also have implications for the mechanistic understanding of conformational switching in other signaling proteins.

AB - The pathogenic pathway of Legionella pneumophila exploits the intercellular vesicle transport system via the posttranslational attachment of adenosine monophosphate (AMP) to the Tyr77 sidechain of human Ras like GTPase Rab1b. The modification, termed adenylylation, is performed by the bacterial enzyme DrrA/SidM, however the effect on conformational properties of the molecular switch mechanism of Rab1b remained unresolved. In this study we find that the adenylylation of Tyr77 stabilizes the active Rab1b state by locking the switch in the active signaling conformation independent of bound GTP or GDP and that electrostatic interactions due to the additional negative charge in the switch region make significant contributions. The stacking interaction between adenine and Phe45 however, seems to have only minor influence on this stabilisation. The results may also have implications for the mechanistic understanding of conformational switching in other signaling proteins.

KW - Adenosine Monophosphate

KW - Guanosine Triphosphate

KW - Molecular Dynamics Simulation

KW - Protein Binding

KW - Protein Conformation

KW - Protein Stability

KW - Static Electricity

KW - Tyrosine

KW - rab1 GTP-Binding Proteins

KW - Journal Article

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

U2 - 10.1038/srep19896

DO - 10.1038/srep19896

M3 - SCORING: Journal article

C2 - 26818796

VL - 6

SP - 19896

JO - SCI REP-UK

JF - SCI REP-UK

SN - 2045-2322

ER -