4PAY

Crystal structure of an N-terminal fragment of the Legionella pneumophila effector protein SidC.

Replaces:  4OM6

Summary for 4PAY

• Entry DOI: 10.2210/pdb4pay/pdb
• Descriptor: SidC, interaptin, BARIUM ION (3 entities in total)
• Functional Keywords: tethering, vesicular transport, legionella pneumophila effector, transport protein
• Biological source: Legionella pneumophila subsp. pneumophila
• Total number of polymer chains: 2
• Total formula weight: 141450.66

Authors

Horenkamp, F.A.,Mukherjee, S.,Alix, E.,Schauder, C.M.,Hubber, A.M.,Roy, C.R.,Reinisch, K.M. (deposition date: 2014-04-10, release date: 2014-06-25, Last modification date: 2024-11-13)

Primary citation

Horenkamp, F.A.,Mukherjee, S.,Alix, E.,Schauder, C.M.,Hubber, A.M.,Roy, C.R.,Reinisch, K.M.
Legionella pneumophila Subversion of Host Vesicular Transport by SidC Effector Proteins.
Traffic, 15:488-499, 2014

PubMed Abstract: Tethering proteins play a key role in vesicular transport, ensuring that cargo arrives at a specific destination. The bacterial effector protein SidC and its paralog SdcA have been described as tethering factors encoded by the intracellular pathogen Legionella pneumophila. Here, we demonstrate that SidC proteins are important for early events unique to maturation of vacuoles containing Legionella and discover monoubiquitination of Rab1 as a new SidC-dependent activity. The crystal structure of the SidC N-terminus revealed a novel fold that is important for function and could be involved in Legionella adaptations to evolutionarily divergent host cells it encounters in natural environments.

PubMed: 24483784
DOI: 10.1111/tra.12158

Experimental method

X-RAY DIFFRACTION (2.77 Å)