5VGC

Crystal structure of the NleG5-1 effector (C200A) from Escherichia coli O157:H7 str. Sakai

5VGC の概要

• エントリーDOI: 10.2210/pdb5vgc/pdb
• 分子名称: NleG5-1 effector, CALCIUM ION, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: ubiquitination, effectors, structural genomics, center for structural genomics of infectious diseases, csgid, protein binding
• 由来する生物種: Enterobacteria phage YYZ-2008
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48864.15

構造登録者

Borek, D.,Valleau, D.,Skarina, T.,Jobin, M.C.,Wawrzak, Z.,Anderson, W.F.,Savchenko, A.,Center for Structural Genomics of Infectious Diseases (CSGID) (登録日: 2017-04-10, 公開日: 2018-04-18, 最終更新日: 2026-02-25)

主引用文献

Valleau, D.,Little, D.J.,Borek, D.,Skarina, T.,Quaile, A.T.,Di Leo, R.,Houliston, S.,Lemak, A.,Arrowsmith, C.H.,Coombes, B.K.,Savchenko, A.
Functional diversification of the NleG effector family in enterohemorrhagic Escherichia coli.
Proc.Natl.Acad.Sci.USA, 115:10004-10009, 2018

PubMed Abstract: The pathogenic strategy of and many other gram-negative pathogens relies on the translocation of a specific set of proteins, called effectors, into the eukaryotic host cell during infection. These effectors act in concert to modulate host cell processes in favor of the invading pathogen. Injected by the type III secretion system (T3SS), the effector arsenal of enterohemorrhagic (EHEC) O157:H7 features at least eight individual NleG effectors, which are also found across diverse attaching and effacing pathogens. NleG effectors share a conserved C-terminal U-box E3 ubiquitin ligase domain that engages with host ubiquitination machinery. However, their specific functions and ubiquitination targets have remained uncharacterized. Here, we identify host proteins targeted for ubiquitination-mediated degradation by two EHEC NleG family members, NleG5-1 and NleG2-3. NleG5-1 localizes to the host cell nucleus and targets the MED15 subunit of the Mediator complex, while NleG2-3 resides in the host cytosol and triggers degradation of Hexokinase-2 and SNAP29. Our structural studies of NleG5-1 reveal a distinct N-terminal α/β domain that is responsible for interacting with host protein targets. The core of this domain is conserved across the NleG family, suggesting this domain is present in functionally distinct NleG effectors, which evolved diversified surface residues to interact with specific host proteins. This is a demonstration of the functional diversification and the range of host proteins targeted by the most expanded effector family in the pathogenic arsenal of .

PubMed: 30217892
DOI: 10.1073/pnas.1718350115

実験手法

X-RAY DIFFRACTION (2.6 Å)