7c7z

Crystal structure of the flagellar junction protein FlgL from Legionella pneumophila

spinqualitylabelsall models 7c7z, resolution 3.06Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7c7z is a 2 chain structure with sequence from Legionella pneumophila. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.06Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5ZW61_LEGPH Publication Abstract from PubMed Legionella pneumophila is a flagellated pathogenic bacterium that causes atypical pneumonia called Legionnaires' disease. The flagellum plays a key role in the pathogenesis of L. pneumophila in the host. The protein FlgL forms a junction between the flagellar hook and filament and has been reported to elicit the host humoral immune response. To provide structural insights into FlgL-mediated junction assembly and FlgL-based vaccine design, we performed structural and serological studies on L. pneumophila FlgL (lpFlgL). The crystal structure of a truncated lpFlgL protein that consists of the D1 and D2 domains was determined at 3.06 A resolution. The D1 domain of lpFlgL adopts a primarily helical, rod-shaped structure, and the D2 domain folds into a beta-sandwich structure that is affixed to the upper region of the D1 domain. The D1 domain of lpFlgL exhibits structural similarity to the flagellar filament protein flagellin, allowing us to propose a structural model of the lpFlgL junction based on the polymeric structure of flagellin. Furthermore, the D1 domain of lpFlgL exhibited substantially higher protein stability than the D2 domain and was responsible for most of the antigenicity of lpFlgL, suggesting that the D1 domain of lpFlgL would be a suitable target for the development of an anti-L. pneumophila vaccine. Structural study of the flagellar junction protein FlgL from Legionella pneumophila.,Song WS, Hong HJ, Yoon SI Biochem Biophys Res Commun. 2020 Aug 20;529(2):513-518. doi:, 10.1016/j.bbrc.2020.06.012. Epub 2020 Jul 4. PMID:32703460 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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