{"entity": "researcher", "timestamp": "2026-08-23T12:57:24.018Z", "family": "Schneider", "given": "Sabine", "initials": "S", "orcid": "0000-0003-1054-8689", "affiliations": ["Department of Chemistry, Center for Integrated Protein Science Munich (CIPSM), Technische Universit\u00e4t M\u00fcnchen, Lichtenbergstra\u00dfe 4, 85747, Garching, Germany."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/6a735346a5ac4603b0f85f3b1112e996.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/6a735346a5ac4603b0f85f3b1112e996"}}, "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"}, {"entity": "publication", "iuid": "90415ee5aa1349ef8a6ec14d830ace32", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/90415ee5aa1349ef8a6ec14d830ace32.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/90415ee5aa1349ef8a6ec14d830ace32"}}, "title": "Selective Activation of Human Caseinolytic Protease P (ClpP).", "authors": [{"family": "Stahl", "given": "Matthias", "initials": "M", "orcid": "0000-0002-0176-9386", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/e51ba23ba70a47bba2d5fa5de3610b2e.json"}}, {"family": "Korotkov", "given": "Vadim S", "initials": "VS", "orcid": "0000-0003-3970-2483", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/99f1fc62226b478a86ac5da5be09e39e.json"}}, {"family": "Balogh", "given": "D\u00f3ra", "initials": "D"}, {"family": "Kick", "given": "Leonhard M", "initials": "LM", "orcid": "0000-0001-5231-208X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/ef2d0aaeaa3843088eee6d460854491a.json"}}, {"family": "Gersch", "given": "Malte", "initials": "M"}, {"family": "Pahl", "given": "Axel", "initials": "A"}, {"family": "Kielkowski", "given": "Pavel", "initials": "P"}, {"family": "Richter", "given": "Klaus", "initials": "K"}, {"family": "Schneider", "given": "Sabine", "initials": "S", "orcid": "0000-0003-1054-8689", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/6a735346a5ac4603b0f85f3b1112e996.json"}}, {"family": "Sieber", "given": "Stephan A", "initials": "SA", "orcid": "0000-0002-9400-906X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/ed221037cc8f4af18984505bc69cd193.json"}}], "type": "journal article", "published": "2018-10-26", "journal": {"title": "Angew. Chem. Int. Ed. Engl.", "issn": "1521-3773", "volume": "57", "issue": "44", "pages": "14602-14607", "issn-l": "1433-7851"}, "abstract": "Caseinolytic protease P (ClpP) is the proteolytic component of the ClpXP protein degradation complex. Eukaryotic ClpP was recently found to act within the mitochondria-specific unfolded protein response (UPRmt ). However, its detailed function and dedicated regulation remain largely unexplored. A small molecule (D9) acts as a potent and species-selective activator of human ClpP (hClpP) by mimicking the natural chaperone ClpX. Structure-activity relationship studies highlight the importance of a halogenated benzyl motif within D9 that interacts with a unique aromatic amino acid network in hClpP. Mutational and structural studies suggest that this YYW motif tightly controls hClpP activity and regulates substrate turnover by interaction with cognate ligands. This signature motif is unique to ClpP from higher organisms and does not exist in tested bacterial homologues, allowing a species-selective analysis. Thus, D9 is a versatile tool to analyze mechanistic features of hClpP.", "doi": "10.1002/anie.201808189", "pmid": "30129683", "labels": [], "xrefs": [], "notes": [], "created": "2026-08-21T11:00:09.220Z", "modified": "2026-08-21T11:00:09.425Z"}]}