Chemical shift assignments of PA2072 CHASE4 domain.

Autor: Duan Y; School of Life Sciences, Tianjin University, Tianjin, 300072, P.R. China., Yuan W; School of Life Sciences, Tianjin University, Tianjin, 300072, P.R. China., Lin Z; School of Life Sciences, Tianjin University, Tianjin, 300072, P.R. China. linzhi@linzhi.net., Zhang Y; School of Life Sciences, Tianjin University, Tianjin, 300072, P.R. China. zhangy2769@mail.sysu.edu.cn.; Present address: The Seventh Affiliated Hospital of Sun Yat-sen University, Shenzhen, 518107, China. zhangy2769@mail.sysu.edu.cn.
Jazyk: angličtina
Zdroj: Biomolecular NMR assignments [Biomol NMR Assign] 2024 Dec; Vol. 18 (2), pp. 305-308. Date of Electronic Publication: 2024 Sep 21.
DOI: 10.1007/s12104-024-10204-3
Abstrakt: Diverse extracellular sensor domains enable cells to regulate their behavior, physiological processes, and interspecies interactions in response to environmental stimuli. These sensing mechanisms facilitate the ultimate adaptation of organisms to their surrounding conditions. Pseudomonas aeruginosa (PAO1) is a clinically significant opportunistic pathogen in hospital infection. The CHASE4 domain, a putative extracellular sensing module, is found in the N-terminus of GGDEF-EAL-containing PA2072, a transmembrane receptor from P. aeruginosa. However, the signal identification and sensing mechanism of monomeric PA2072 CHASE4 remains largely unknown. Here, we report backbone and side chain resonance assignments of PA2072 CHASE4 as a basis for studying the structural mechanism of CHASE4-mediated signal recognition.
(© 2024. The Author(s), under exclusive licence to Springer Nature B.V.)
Databáze: MEDLINE
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