8ANP
Legionella effector Lem3 mutant D190A in complex with Mg2+
Summary for 8ANP
| Entry DOI | 10.2210/pdb8anp/pdb |
| Related | 8AGG 8ALK |
| Descriptor | Phosphocholine hydrolase Lem3, MAGNESIUM ION, TRIETHYLENE GLYCOL, ... (5 entities in total) |
| Functional Keywords | legionella effector lem3 displaces the switch ii region of rab1b for dephosphocholination, metal binding protein |
| Biological source | Legionella pneumophila |
| Total number of polymer chains | 4 |
| Total formula weight | 213116.03 |
| Authors | Kaspers, M.S.,Pogenberg, V.,Ernst, S.,Ecker, F.,Pett, C.,Ochtrop, P.,Hedberg, C.,Groll, M.,Itzen, A. (deposition date: 2022-08-05, release date: 2023-04-12, Last modification date: 2024-10-09) |
| Primary citation | Kaspers, M.S.,Pogenberg, V.,Pett, C.,Ernst, S.,Ecker, F.,Ochtrop, P.,Groll, M.,Hedberg, C.,Itzen, A. Dephosphocholination by Legionella effector Lem3 functions through remodelling of the switch II region of Rab1b. Nat Commun, 14:2245-2245, 2023 Cited by PubMed Abstract: Bacterial pathogens often make use of post-translational modifications to manipulate host cells. Legionella pneumophila, the causative agent of Legionnaires disease, secretes the enzyme AnkX that uses cytidine diphosphate-choline to post-translationally modify the human small G-Protein Rab1 with a phosphocholine moiety at Ser76. Later in the infection, the Legionella enzyme Lem3 acts as a dephosphocholinase, hydrolytically removing the phosphocholine. While the molecular mechanism for Rab1 phosphocholination by AnkX has recently been resolved, structural insights into the activity of Lem3 remained elusive. Here, we stabilise the transient Lem3:Rab1b complex by substrate mediated covalent capture. Through crystal structures of Lem3 in the apo form and in complex with Rab1b, we reveal Lem3's catalytic mechanism, showing that it acts on Rab1 by locally unfolding it. Since Lem3 shares high structural similarity with metal-dependent protein phosphatases, our Lem3:Rab1b complex structure also sheds light on how these phosphatases recognise protein substrates. PubMed: 37076474DOI: 10.1038/s41467-023-37621-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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