6d7r

Crystal structure of an inactivate variant of the quorum-sensing master regulator HapR from protease-deficient non-O1, non-O139 Vibrio cholerae strain V2

spinqualitylabelsall models 6d7r, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6d7r is a 2 chain structure with sequence from Vibrio cholerae. This structure supersedes the now removed PDB entry 5l0x. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B2CKP3_VIBCL Publication Abstract from PubMed HapR is a TetR-family transcriptional regulator that controls quorum sensing in Vibrio cholerae, the causative agent of cholera. HapR regulates the expression of hemagglutinin protease, virulence and biofilm genes. The crystal structure of wild-type HapR from V. cholerae strain O1 El Tor C6706 has previously been solved. In this study, the structure of a DNA-binding-deficient variant of HapR (HapRV2) derived from the protease-deficient V. cholerae serotype O37 strain V2 is reported. The structure reveals no structural differences compared with wild-type HapR. However, structural alignment of HapRV2 with the TetR-family member QacR in complex with its operator DNA suggests that the aspartate residue located between the regulatory and DNA-binding domains may clash with and electrostatically repel the phosphate backbone of DNA to prevent binding. Crystal structure of an inactive variant of the quorum-sensing master regulator HapR from the protease-deficient non-O1, non-O139 Vibrio cholerae strain V2.,Cruite J, Succo P, Raychaudhuri S, Kull FJ Acta Crystallogr F Struct Biol Commun. 2018 Jun 1;74(Pt 6):331-336. doi:, 10.1107/S2053230X18006519. Epub 2018 May 17. PMID:29870016 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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