{"entity": "researcher", "timestamp": "2026-08-23T12:57:00.291Z", "family": "Itzen", "given": "Aymelt", "initials": "A", "orcid": "0000-0002-4249-5617", "affiliations": ["Center for Integrated Protein Science Munich (CIPSM), Department of Chemistry, Technical University of Munich, Garching, 85748, Germany. a.itzen@uke.de.", "Center for Experimental Medicine, Institute of Biochemistry and Signal Transduction, Universit\u00e4tsklinikum Hamburg-Eppendorf (UKE), Hamburg, 20246, Germany. a.itzen@uke.de.", "Center for Structural Systems Biology (CSSB), University Medical Centre Hamburg-Eppendorf (UKE), Hamburg, Germany. a.itzen@uke.de."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/831977b2fbac49269c0ada6144bc65dc.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/831977b2fbac49269c0ada6144bc65dc"}}, "publications": [{"entity": "publication", "iuid": "eada2ce2db024ef2b7445d40b2481dcd", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/eada2ce2db024ef2b7445d40b2481dcd.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/eada2ce2db024ef2b7445d40b2481dcd"}}, "title": "Rab1-AMPylation by Legionella DrrA is allosterically activated by Rab1.", "authors": [{"family": "Du", "given": "Jiqing", "initials": "J", "orcid": "0000-0002-2940-3925", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/706d85fe86054072beb17874fc02c90e.json"}}, {"family": "Wrisberg", "given": "Marie-Kristin von", "initials": "MV", "orcid": "0000-0002-7100-4565", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/403af701a74c405aa354146ab3e58ab9.json"}}, {"family": "Gulen", "given": "Burak", "initials": "B", "orcid": "0000-0003-2945-3428", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/6dc1ca7e458543a586b5d3cc5b15bf5b.json"}}, {"family": "Stahl", "given": "Matthias", "initials": "M", "orcid": "0000-0002-0176-9386", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/e51ba23ba70a47bba2d5fa5de3610b2e.json"}}, {"family": "Pett", "given": "Christian", "initials": "C", "orcid": "0000-0001-7039-7312", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/4f0d2a51c0fb4395816b7153932503b9.json"}}, {"family": "Hedberg", "given": "Christian", "initials": "C"}, {"family": "Lang", "given": "Kathrin", "initials": "K", "orcid": "0000-0002-1318-6567", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/f7c04dc7c380470498ed008955868b97.json"}}, {"family": "Schneider", "given": "Sabine", "initials": "S", "orcid": "0000-0003-1054-8689", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/6a735346a5ac4603b0f85f3b1112e996.json"}}, {"family": "Itzen", "given": "Aymelt", "initials": "A", "orcid": "0000-0002-4249-5617", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/831977b2fbac49269c0ada6144bc65dc.json"}}], "type": "journal article", "published": "2021-01-19", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "12", "issue": "1", "pages": "460", "issn-l": "2041-1723"}, "abstract": "Legionella pneumophila infects eukaryotic cells by forming a replicative organelle - the Legionella containing vacuole. During this process, the bacterial protein DrrA/SidM is secreted and manipulates the activity and post-translational modification (PTM) states of the vesicular trafficking regulator Rab1. As a result, Rab1 is modified with an adenosine monophosphate (AMP), and this process is referred to as AMPylation. Here, we use a chemical approach to stabilise low-affinity Rab:DrrA complexes in a site-specific manner to gain insight into the molecular basis of the interaction between the Rab protein and the AMPylation domain of DrrA. The crystal structure of the Rab:DrrA complex reveals a previously unknown non-conventional Rab-binding site (NC-RBS). Biochemical characterisation demonstrates allosteric stimulation of the AMPylation activity of DrrA via Rab binding to the NC-RBS. We speculate that allosteric control of DrrA could in principle prevent random and potentially cytotoxic AMPylation in the host, thereby perhaps ensuring efficient infection by Legionella.", "doi": "10.1038/s41467-020-20702-2", "pmid": "33469029", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC7815794"}, {"db": "pii", "key": "10.1038/s41467-020-20702-2"}], "notes": [], "created": "2026-08-21T11:48:54.410Z", "modified": "2026-08-21T11:48:54.806Z"}]}