5K34

Structure of the ankyrin domain of AnkB from Legionella Pneumophila

Summary for 5K34

• Entry DOI: 10.2210/pdb5k34/pdb
• Related: 5K35
• Descriptor: Ankyrin-repeat protein B, GLYCEROL, SULFATE ION, ... (4 entities in total)
• Functional Keywords: bacterial effector, ankyrin domain, protein-protein interaction, structural genomics, montreal-kingston bacterial structural genomics initiative, bsgi, protein binding
• Biological source: Legionella pneumophila
• Total number of polymer chains: 1
• Total formula weight: 13957.05

Authors

Wong, K.,Kozlov, G.,Gehring, K.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2016-05-19, release date: 2017-01-25, Last modification date: 2024-03-06)

Primary citation

Wong, K.,Perpich, J.D.,Kozlov, G.,Cygler, M.,Abu Kwaik, Y.,Gehring, K.
Structural Mimicry by a Bacterial F Box Effector Hijacks the Host Ubiquitin-Proteasome System.
Structure, 25:376-383, 2017

PubMed Abstract: Ankyrin B (AnkB/LegAU13) is a translocated F box effector essential for the intracellular replication of the pathogen Legionella pneumophila. AnkB co-opts a host ubiquitin ligase to decorate the pathogen-containing vacuole with K-linked polyubiquitinated proteins and degrade host proteins as a source of energy. Here, we report that AnkB commandeers the host ubiquitin-proteasome system through mimicry of two eukaryotic protein domains. Using X-ray crystallography, we determined the 3D structure of AnkB in complex with Skp1, a component of the human SCF ubiquitination ligase. The structure confirms that AnkB contains an N-terminal F box similar to Skp2 and a C-terminal substrate-binding domain similar to eukaryotic ankyrin repeats. We identified crucial amino acids in the substrate-binding domain of AnkB and showed them to be essential for the function of AnkB in L. pneumophila intracellular proliferation. The study reveals how Legionella uses molecular mimicry to manipulate the host ubiquitination pathway and proliferate intracellularly.

PubMed: 28111017
DOI: 10.1016/j.str.2016.12.015

Experimental method

X-RAY DIFFRACTION (1.15 Å)