5HAF
Structure of Salmonella enterica effector protein SseL
5HAF の概要
| エントリーDOI | 10.2210/pdb5haf/pdb |
| 分子名称 | Deubiquitinase SseL, POTASSIUM ION (3 entities in total) |
| 機能のキーワード | enzyme, ce clan, deubiquitinase, hydrolase |
| 由来する生物種 | Salmonella enterica subsp. enterica serovar Typhimurium |
| 細胞内の位置 | Secreted: Q8ZNG2 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 75758.33 |
| 構造登録者 | |
| 主引用文献 | Pruneda, J.N.,Durkin, C.H.,Geurink, P.P.,Ovaa, H.,Santhanam, B.,Holden, D.W.,Komander, D. The Molecular Basis for Ubiquitin and Ubiquitin-like Specificities in Bacterial Effector Proteases. Mol.Cell, 63:261-276, 2016 Cited by PubMed Abstract: Pathogenic bacteria rely on secreted effector proteins to manipulate host signaling pathways, often in creative ways. CE clan proteases, specific hydrolases for ubiquitin-like modifications (SUMO and NEDD8) in eukaryotes, reportedly serve as bacterial effector proteins with deSUMOylase, deubiquitinase, or, even, acetyltransferase activities. Here, we characterize bacterial CE protease activities, revealing K63-linkage-specific deubiquitinases in human pathogens, such as Salmonella, Escherichia, and Shigella, as well as ubiquitin/ubiquitin-like cross-reactive enzymes in Chlamydia, Rickettsia, and Xanthomonas. Five crystal structures, including ubiquitin/ubiquitin-like complexes, explain substrate specificities and redefine relationships across the CE clan. Importantly, this work identifies novel family members and provides key discoveries among previously reported effectors, such as the unexpected deubiquitinase activity in Xanthomonas XopD, contributed by an unstructured ubiquitin binding region. Furthermore, accessory domains regulate properties such as subcellular localization, as exemplified by a ubiquitin-binding domain in Salmonella Typhimurium SseL. Our work both highlights and explains the functional adaptations observed among diverse CE clan proteins. PubMed: 27425412DOI: 10.1016/j.molcel.2016.06.015 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.7 Å) |
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