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
Replaces: 5L0XSummary for 6D7R
Entry DOI | 10.2210/pdb6d7r/pdb |
Descriptor | Hemagglutinin/protease regulatory protein (2 entities in total) |
Functional Keywords | tetr, quorum-sensing, transcription |
Biological source | Vibrio cholerae |
Total number of polymer chains | 2 |
Total formula weight | 51903.60 |
Authors | Cruite, J.T.,Succo, P.,Raychaudhuri, S.,Kull, F.J. (deposition date: 2018-04-25, release date: 2018-05-30, Last modification date: 2024-11-20) |
Primary citation | Cruite, J.,Succo, P.,Raychaudhuri, S.,Kull, F.J. 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. Acta Crystallogr F Struct Biol Commun, 74:331-336, 2018 Cited by PubMed Abstract: 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 (HapR) 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 HapR 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. PubMed: 29870016DOI: 10.1107/S2053230X18006519 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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