7bwk | pdb_00007bwk

Structure of DotL(656-783)-IcmS-IcmW-LvgA-VpdB(461-590) derived from Legionella pneumophila

spinqualitylabelsall models 7bwk, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7bwk is a 10 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 2.801Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DOTL_LEGPH Component of the Dot/Icm type IVB secretion system (T4BSS), which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:17040490, PubMed:22694730, PubMed:32513920). Part of a subcomplex which recruits effector proteins and delivers them to the core transmembrane subcomplex (PubMed:23028312, PubMed:32513920). Plays a central role in the assembly of the subcomplex (PubMed:32513920). Required for the recruitment of IcmS and IcmW to the inner membrane and for the translocation of adapter-dependent substrates (PubMed:23028312). May have ATPase activity (Probable). Publication Abstract from PubMed The Legionella pneumophila Dot/Icm type IVB secretion system (T4BSS) is extremely versatile, translocating ~300 effector proteins into host cells. This specialized secretion system employs the Dot/Icm type IVB coupling protein (T4CP) complex, which includes IcmS, IcmW and LvgA, that are known to selectively assist the export of a subclass of effectors. Herein, the crystal structure of a four-subunit T4CP subcomplex bound to the effector protein VpdB reveals an interaction between LvgA and a linear motif in the C-terminus of VpdB. The same binding interface of LvgA also interacts with the C-terminal region of three additional effectors, SidH, SetA and PieA. Mutational analyses identified a FxxxLxxxK binding motif that is shared by VpdB and SidH, but not by SetA and PieA, showing that LvgA recognizes more than one type of binding motif. Together, this work provides a structural basis for how the Dot/Icm T4CP complex recognizes effectors, and highlights the multiple substrate-binding specificities of its adaptor subunit. Structural basis for effector protein recognition by the Dot/Icm Type IVB coupling protein complex.,Kim H, Kubori T, Yamazaki K, Kwak MJ, Park SY, Nagai H, Vogel JP, Oh BH Nat Commun. 2020 May 26;11(1):2623. doi: 10.1038/s41467-020-16397-0. PMID:32457311 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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