7BWK
Structure of DotL(656-783)-IcmS-IcmW-LvgA-VpdB(461-590) derived from Legionella pneumophila
Summary for 7BWK
| Entry DOI | 10.2210/pdb7bwk/pdb |
| Descriptor | IcmO (DotL), IcmS, IcmW, ... (5 entities in total) |
| Functional Keywords | dot/icm type 4b secretion system, effector recognition, type 4b coupling protein complex-effector complex, dotl-icmsw-lvga, vpdb, protein transport |
| Biological source | Legionella pneumophila subsp. pneumophila str. Philadelphia 1 More |
| Total number of polymer chains | 10 |
| Total formula weight | 165249.83 |
| Authors | Kim, H.,Kwak, M.J.,Oh, B.H. (deposition date: 2020-04-14, release date: 2020-06-03, Last modification date: 2023-11-29) |
| Primary citation | Kim, H.,Kubori, T.,Yamazaki, K.,Kwak, M.J.,Park, S.Y.,Nagai, H.,Vogel, J.P.,Oh, B.H. Structural basis for effector protein recognition by the Dot/Icm Type IVB coupling protein complex. Nat Commun, 11:2623-2623, 2020 Cited by PubMed Abstract: 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. PubMed: 32457311DOI: 10.1038/s41467-020-16397-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.801 Å) |
Structure validation
Download full validation report
