6VPW

1.90 Angstrom Resolution Crystal Structure Chemotaxis protein CheX from Vibrio vulnificus

Summary for 6VPW

• Entry DOI: 10.2210/pdb6vpw/pdb
• Descriptor: Chemotaxis protein CheX (2 entities in total)
• Functional Keywords: structural genomics, center for structural genomics of infectious diseases, csgid, signaling protein
• Biological source: Vibrio vulnificus (strain CMCP6)
• Total number of polymer chains: 2
• Total formula weight: 33710.91

Authors

Minasov, G.,Shuvalova, L.,Kiryukhina, O.,Wiersum, G.,Endres, M.,Satchell, K.J.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2020-02-04, release date: 2021-02-10, Last modification date: 2026-01-28)

Primary citation

Frederick, A.,Lopes, C.,Fulton, B.,Huang, Y.,Podicheti, R.,Rusch, D.,Minasov, G.,Shuvalova, L.,Satchell, K.J.F.,Rowe-Magnus, D.A.
Altering chemotaxis as a strategy to enhance the foraging range of motility-restricted bacteria.
Commun Biol, 2026

PubMed Abstract: Chemotaxis is an adaptive mechanism that shapes the behavior of motile bacteria in habitats characterized by fluctuating and often conflicting cues environmental (e.g. stay-or-go). Chemotactic responses are orchestrated by phosphorylation of CheY, which triggers rotational switching of the flagella. In Escherichia coli and similar taxa, CheZ is the principal CheY-P phosphatase, whereas in lineages lacking CheZ, members of the structurally distinct CheC-FliY-CheX family fulfill this role. Intriguingly, some bacteria code for CheX and CheZ, presenting a conundrum regarding their function, and the role of CheX in CheZ-containing organisms is unknown. We imposed a sustained motility constraint under conditions of looming nutrient depletion in Vibrio vulnificus, which possesses both CheX and CheZ, using the c-di-GMP effector PlzD that robustly curtails swimming motility. Our analyses revealed that the activity of CheX, but not CheZ, could be attenuated to mitigate the imposed constraint, assigning CheX a pivotal function in fine-tuning foraging behavior during a "stay-or-go" decision. V. vulnificus CheX maintained CheY-P phosphatase activity despite its conserved dimeric fold structure exhibiting divergence in active-site architecture, suggesting a preserved catalytic mechanism among distantly related homologs. Co-conservation of cheX and cheZ across disparate bacterial phyla suggests their adaptative retention confers robustness and versatility to chemotactic control.

PubMed: 41495260
DOI: 10.1038/s42003-025-09475-w

Experimental method

X-RAY DIFFRACTION (1.9 Å)