6kju

Huge conformation shift of Vibrio cholerae VqmA dimer in the absence of target DNA provides insight into DNA-binding mechanisms of LuxR-type receptors

spinqualitylabelsall models 6kju, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6kju is a 2 chain structure with sequence from Vibrio cholerae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.75Å Ligands: A1U Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9KKM5_VIBCH Publication Abstract from PubMed Quorum sensing regulates the biofilm formation and expression of virulence factors in Vibrio cholerae, an obligate human pathogen that continues to imperil human health. Cytoplasmic transcription factor VqmA is a LuxR-type receptor ubiquitous in the Vibrio genus and one vibriophage VP882 and plays an important role in V. cholerae pathogenicity. Here we presented the X-ray crystal structure of V. cholerae VqmA-DPO complex and compared it with the previously determined VqmA-DPO-DNA complex. To our knowledge, this is the first report on the crystal structures of the same LuxR-type receptor with two conformations of binding to DNA and not binding to DNA. Based on the results of structural analysis and biochemical assays, we revealed the secondary structure of the linker region between two function domains changed significantly, and DNA binding domains were covalently linked by a disulfide bond formed by the highly conserved Cys134. Besides, the distance between two DBD monomers became longer than that in DNA-binding conformation, and two alpha8 helixes underwent a large conformation shift. The results of the structure-function analyses presented here improve our understanding of the complex mechanisms in the conformational changes of LuxR-type receptors caused by DNA binding. Large conformation shifts of Vibrio cholerae VqmA dimer in the absence of target DNA provide insight into DNA-binding mechanisms of LuxR-type receptors.,Wu H, Li M, Peng C, Yin Y, Guo H, Wang W, Xu Q, Zhou H, Xu C, Yu F, He J Biochem Biophys Res Commun. 2019 Dec 3;520(2):399-405. doi:, 10.1016/j.bbrc.2019.10.063. Epub 2019 Oct 9. PMID:31606206 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transcriptional activator 3D structures

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