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6A51

Novel Regulators CheP and CheQ Specifically Control Chemotaxis Core Gene cheVAW Transcription in Bacterial Pathogen Campylobacter jejuni

Summary for 6A51
Entry DOI10.2210/pdb6a51/pdb
DescriptorCheQ (2 entities in total)
Functional Keywordschemotaxis, gene regulation, campylobacter, hdod domain, unknown function
Biological sourceCampylobacter jejuni subsp. jejuni
Total number of polymer chains2
Total formula weight39770.13
Authors
Lu, G.,Gao, B.,Cha, G.,Chen, Z.,Mo, R. (deposition date: 2018-06-21, release date: 2019-06-26, Last modification date: 2024-11-06)
Primary citationCha, G.,Chen, Z.,Mo, R.,Lu, G.,Gao, B.
The novel regulators CheP and CheQ control the core chemotaxis operon cheVAW in Campylobacter jejuni.
Mol.Microbiol., 111:145-158, 2019
Cited by
PubMed Abstract: Campylobacter jejuni is the leading cause of foodborne gastrointestinal illness worldwide, and chemotaxis plays an important role in its host colonization and pathogenesis. Although many studies on chemotaxis have focused on the physical organization and signaling mechanism of the system's protein complex, much less is known about the transcriptional regulation of its components. Here, we describe two novel regulators, CJJ81176_0275 and CJJ81176_0276 (designated as CheP and CheQ), which specifically activate the transcription of the chemotaxis core genes cheV, cheA and cheW in C. jejuni and they are also essential for chemotactic responses. CheP has a single HD-related output domain (HDOD) domain and can promote CheQ binding to the cheVAW operon promoter through a protein-protein interaction. Mutagenesis analyses identified key residues critical for CheP function and/or interaction with CheQ. Further structural characterization of CheQ revealed a novel fold with strong positive surface charges that allow for its DNA binding. These findings reveal the gene regulatory mechanism of the chemotaxis system in an important bacterial pathogen and provide potential anti-virulence targets for campylobacteriosis treatment. In addition, ChePQ is an example of how proteins with the widespread but functionally obscure HDOD can coordinate with a signal output DNA-binding protein/domain to regulate the expression of important signaling pathways.
PubMed: 30338872
DOI: 10.1111/mmi.14144
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

239492

数据于2025-07-30公开中

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