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4om6 is a 2 chain structure with sequence from Legph. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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.
Legionella pneumophila Subversion of Host Vesicular Transport by SidC Effector Proteins.,Horenkamp FA, Mukherjee S, Alix E, Schauder CM, Hubber AM, Roy CR, Reinisch KM Traffic. 2014 May;15(5):488-99. doi: 10.1111/tra.12158. Epub 2014 Mar 12. PMID:24483784[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Horenkamp FA, Mukherjee S, Alix E, Schauder CM, Hubber AM, Roy CR, Reinisch KM. Legionella pneumophila Subversion of Host Vesicular Transport by SidC Effector Proteins. Traffic. 2014 May;15(5):488-99. doi: 10.1111/tra.12158. Epub 2014 Mar 12. PMID:24483784 doi:http://dx.doi.org/10.1111/tra.12158
