5MS2

Crystal structure of the Legionella pneumophila effector protein RavZ in complex with human LC3B

Summary for 5MS2

• Entry DOI: 10.2210/pdb5ms2/pdb
• Descriptor: Legionella pneumophila effector protein RavZ, Microtubule-associated proteins 1A/1B light chain 3B (3 entities in total)
• Functional Keywords: hydrolase, autophagy, host-pathogen interaction
• Biological source: Legionella pneumophila subsp. pneumophila str. Philadelphia 1; More
• Total number of polymer chains: 2
• Total formula weight: 63103.23

Authors

Pantoom, S.,Vetter, I.R.,Wu, Y.W. (deposition date: 2016-12-30, release date: 2017-04-19, Last modification date: 2024-01-17)

Primary citation

Yang, A.,Pantoom, S.,Wu, Y.W.
Elucidation of the anti-autophagy mechanism of the Legionella effector RavZ using semisynthetic LC3 proteins.
Elife, 6:-, 2017

PubMed Abstract: Autophagy is a conserved cellular process involved in the elimination of proteins and organelles. It is also used to combat infection with pathogenic microbes. The intracellular pathogen manipulates autophagy by delivering the effector protein RavZ to deconjugate Atg8/LC3 proteins coupled to phosphatidylethanolamine (PE) on autophagosomal membranes. To understand how RavZ recognizes and deconjugates LC3-PE, we prepared semisynthetic LC3 proteins and elucidated the structures of the RavZ:LC3 interaction. Semisynthetic LC3 proteins allowed the analysis of structure-function relationships. RavZ extracts LC3-PE from the membrane before deconjugation. RavZ initially recognizes the LC3 molecule on membranes via its N-terminal LC3-interacting region (LIR) motif. The RavZ α3 helix is involved in extraction of the PE moiety and docking of the acyl chains into the lipid-binding site of RavZ that is related in structure to that of the phospholipid transfer protein Sec14. Thus, has evolved a novel mechanism to specifically evade host autophagy.

PubMed: 28395732
DOI: 10.7554/eLife.23905

Experimental method

X-RAY DIFFRACTION (2.47 Å)