5IZV: Crystal Structure Of The Legionella Pneumophila Effector Protein Ravz - F222

Citation:
Abstract
Hosts utilize macroautophagy/autophagy to clear invading bacteria; however, bacteria have also developed a specific mechanism to survive by manipulating the host cell autophagy mechanism. One pathogen, Legionella pneumophila, can hinder host cell autophagy by using the specific effector protein RavZ that cleaves phosphatidylethanolamine-conjugated LC3 on the phagophore membrane. However, the detailed molecular mechanisms associated with the function of RavZ have hitherto remained unclear. Here, we report on the biochemical characteristics of the RavZ-LC3 interaction, the solution structure of the 1:2 complex between RavZ and LC3, and crystal structures of RavZ showing different conformations of the active site loop without LC3. Based on our biochemical, structural, and cell-based analyses of RavZ and LC3, both distant flexible N- and C-terminal regions containing LC3-interacting region (LIR) motifs are important for substrate recognition. These results suggest a novel mechanism of RavZ action on the phagophore membrane and lay the groundwork for understanding how bacterial pathogens can survive autophagy.
PDB ID: 5IZVDownload
MMDB ID: 144729
PDB Deposition Date: 2016/3/26
Updated in MMDB: 2016/11
Experimental Method:
x-ray diffraction
Resolution: 2.81  Å
Source Organism:
Similar Structures:
Biological Unit for 5IZV: monomeric; determined by author
Molecular Components in 5IZV
Label Count Molecule
Protein (1 molecule)
1
Uncharacterized Protein Ravz
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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