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5HAG

Structure of Chlamydia trachomatis effector protein ChlaDUB1

Summary for 5HAG
Entry DOI10.2210/pdb5hag/pdb
DescriptorDeubiquitinase and deneddylase Dub1, GLYCEROL (3 entities in total)
Functional Keywordsenzyme, ce clan, deubiquitinase, acetyltransferase, hydrolase
Biological sourceChlamydia trachomatis
Cellular locationSecreted : B0B9A0
Total number of polymer chains1
Total formula weight31399.34
Authors
Pruneda, J.N.,Komander, D. (deposition date: 2015-12-30, release date: 2016-07-27, Last modification date: 2024-05-08)
Primary citationPruneda, 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: 27425412
DOI: 10.1016/j.molcel.2016.06.015
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

226707

數據於2024-10-30公開中

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