9EMK の概要
| エントリーDOI | 10.2210/pdb9emk/pdb |
| 分子名称 | Septation initiation protein, Polyubiquitin-B, [(2~{R},3~{S},4~{R},5~{S})-5-[(1-ethyl-1,2,3-triazol-4-yl)methoxy]-3,4-bis(oxidanyl)oxolan-2-yl]methyl ethanesulfonate, ... (4 entities in total) |
| 機能のキーワード | covalent complex, chemical warhead, ubiquitin enzyme, infection, unknown function |
| 由来する生物種 | Legionella pneumophila subsp. pneumophila 詳細 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 144979.89 |
| 構造登録者 | |
| 主引用文献 | Kloet, M.S.,Mukhopadhyay, R.,Mukherjee, R.,Misra, M.,Jeong, M.,Talavera Ormeno, C.M.P.,Moutsiopoulou, A.,Tjokrodirijo, R.T.N.,van Veelen, P.A.,Shin, D.,Dikic, I.,Sapmaz, A.,Kim, R.Q.,van der Heden van Noort, G.J. Covalent Probes To Capture Legionella pneumophila Dup Effector Enzymes. J.Am.Chem.Soc., 146:26957-26964, 2024 Cited by PubMed Abstract: Upon infection of host cells, releases a multitude of effector enzymes into the cell's cytoplasm that hijack a plethora of cellular activities, including the host ubiquitination pathways. Effectors belonging to the SidE-family are involved in noncanonical serine phosphoribosyl ubiquitination of host substrate proteins contributing to the formation of a Legionella-containing vacuole that is crucial in the onset of Legionnaires' disease. This dynamic process is reversed by effectors called Dups that hydrolyze the phosphodiester in the phosphoribosyl ubiquitinated protein. We installed reactive warheads on chemically prepared ribosylated ubiquitin to generate a set of probes targeting these Legionella enzymes. In vitro tests on recombinant DupA revealed that a vinyl sulfonate warhead was most efficient in covalent complex formation. Mutagenesis and X-ray crystallography approaches were used to identify the site of covalent cross-linking to be an allosteric cysteine residue. The subsequent application of this probe highlights the potential to selectively enrich the Dup enzymes from Legionella-infected cell lysates. PubMed: 39288007DOI: 10.1021/jacs.4c08168 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.17 Å) |
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