4MU6
Crystal Structure of the N-terminal domain of Effector Protein LegC3 from Legionella pneumophila
Summary for 4MU6
| Entry DOI | 10.2210/pdb4mu6/pdb |
| Descriptor | Kinectin 1 (Kinesin receptor) (2 entities in total) |
| Functional Keywords | structural genomics, unknown function |
| Biological source | Legionella pneumophila |
| Total number of polymer chains | 1 |
| Total formula weight | 42789.26 |
| Authors | Yao, D.,Cherney, M.,Cygler, M. (deposition date: 2013-09-20, release date: 2013-12-11, Last modification date: 2024-11-06) |
| Primary citation | Yao, D.,Cherney, M.,Cygler, M. Structure of the N-terminal domain of the effector protein LegC3 from Legionella pneumophila. Acta Crystallogr.,Sect.D, 70:436-441, 2014 Cited by PubMed Abstract: 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 α-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. PubMed: 24531477DOI: 10.1107/S139900471302991X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.082 Å) |
Structure validation
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