6VPW

1.90 Angstrom Resolution Crystal Structure Chemotaxis protein CheX from Vibrio vulnificus

6VPW の概要

• エントリーDOI: 10.2210/pdb6vpw/pdb
• 分子名称: Chemotaxis protein CheX (2 entities in total)
• 機能のキーワード: structural genomics, center for structural genomics of infectious diseases, csgid, signaling protein
• 由来する生物種: Vibrio vulnificus (strain CMCP6)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 33710.91

構造登録者

Minasov, G.,Shuvalova, L.,Kiryukhina, O.,Wiersum, G.,Endres, M.,Satchell, K.J.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (登録日: 2020-02-04, 公開日: 2021-02-10, 最終更新日: 2026-01-28)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.9 Å)