4mu6

Crystal Structure of the N-terminal domain of Effector Protein LegC3 from Legionella pneumophila

spinqualitylabelsall models 4mu6, resolution 2.08Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4mu6 is a 1 chain structure with sequence from Legionella pneumophila subsp. pneumophila str. Philadelphia 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.082Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5ZUU1_LEGPH Publication Abstract from PubMed Legionella pneumophila secretes over 300 effectors during the invasion of human cells. The functions of only a small number of them have been identified. LegC3 is one of the identified effectors, which is believed to act by inhibiting vacuolar fusion. It contains two predicted transmembrane helices that divide the protein into a larger N-terminal domain and a smaller C-terminal domain. The function of LegC3 has been shown to be associated primarily with the N-terminal domain, which contains coiled-coil sequence motifs. The structure of the N-terminal domain has been determined and it is shown that it is highly alpha-helical and contains a helical bundle followed by a long antiparallel coiled-coil. No similar protein fold has been observed in the PDB. A long loop at the tip of the coiled-coil distal from the membrane is disordered and may be important for interaction with an as yet unidentified protein. Structure of the N-terminal domain of the effector protein LegC3 from Legionella pneumophila.,Yao D, Cherney M, Cygler M Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):436-41. doi:, 10.1107/S139900471302991X. Epub 2014 Jan 29. PMID:24531477 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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