4pay

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

spinqualitylabelsall models 4pay, resolution 2.77Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pay is a 2 chain structure with sequence from Legionella pneumophila subsp. pneumophila str. Philadelphia 1. This structure supersedes the now removed PDB entry 4om6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.77Å Ligands: BA, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5ZSK6_LEGPH Publication Abstract from PubMed 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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