ArticleScientific reports2016
Adenylylation of Tyr77 stabilizes Rab1b GTPase in an active state: A molecular dynamics simulation analysis.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Characterizing host-microbe interactions with bacterial effector proteins using proximity-dependent biotin identification (BioID).Communications biology · 2025Review
- AMPylation of small GTPases by Fic enzymes.FEBS letters · 2023Review
- Rab1-AMPylation by Legionella DrrA is allosterically activated by Rab1.Nature communications · 2021Article
- Conformational control of small GTPases by AMPylation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Directing Traffic: Regulation of COPI Transport by Post-translational Modifications.Frontiers in cell and developmental biology · 2019Review
- Allosteric Activation of GDP-Bound Ras Isoforms by Bisphenol Derivative Plasticisers.International journal of molecular sciences · 2018Article
- Enzymes Involved in AMPylation and deAMPylation.Chemical reviews · 2018Review
- Effects of pH and Salt Concentration on Stability of a Protein G Variant Using Coarse-Grained Models.Biophysical journal · 2018Article
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5 authors.
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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.
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