Zobrazeno 1 - 10
of 37
pro vyhledávání: '"Kylie J. Watts"'
Autor:
Davi R. Ortega, Wen Yang, Poorna Subramanian, Petra Mann, Andreas Kjær, Songye Chen, Kylie J. Watts, Sahand Pirbadian, David A. Collins, Romain Kooger, Marina G. Kalyuzhnaya, Simon Ringgaard, Ariane Briegel, Grant J. Jensen
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
Bacterial chemosensory systems are grouped into 17 flagellar classes (F1-17). Here the authors employ electron cryotomography and comparative genomics to characterise the chemosensory arrays in γ-proteobacteria and identify a structural distinct for
Externí odkaz:
https://doaj.org/article/fd317ed2ceab43ea8273e0e5054c8c8f
Publikováno v:
Molecular microbiologyREFERENCES.
The marine pathogen Vibrio vulnificus senses and responds to environmental stimuli via two chemosensory systems and 42-53 chemoreceptors. Here, we present an analysis of the V. vulnificus Aer2 chemoreceptor, VvAer2, which is the first V. vulnificus c
Publikováno v:
Biochemistry. 60:2610-2622
The Aer2 receptor from Pseudomonas aeruginosa has an O2-binding PAS-heme domain that stabilizes O2 via a Trp residue in the distal heme pocket. Trp rotates ∼90° to bond with the ligand and initiate signaling. Although the isolated PAS domain is mo
Publikováno v:
Curr Opin Microbiol
PAS domains are widespread, versatile domains found in proteins from all kingdoms of life. The PAS fold is composed of an antiparallel β-sheet with several flanking α-helices, and contains a conserved cleft for cofactor or ligand binding. The last
Publikováno v:
J Bacteriol
The Aer2 chemoreceptor from Pseudomonas aeruginosa is an Osub2/subsensor involved in stress responses, virulence, and tuning the behavior of the chemotaxis (Che) system. Aer2 is the sole receptor of the Che2 system. It is soluble, but membrane associ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0be03f34f0b7bb95d38a969f75c9b8b
https://europepmc.org/articles/PMC9487508/
https://europepmc.org/articles/PMC9487508/
Autor:
Emilie Orillard, Kylie J. Watts
Publikováno v:
J Bacteriol
In this study, we provide the first characterization of a chemoreceptor from Leptospira interrogans, the cause of leptospirosis. This receptor is related to the Aer2 receptors that have been studied in other bacteria. In those organisms, Aer2 is a so
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7dcb52bd281ee0551d4b3c77367c2c0d
https://europepmc.org/articles/PMC9017314/
https://europepmc.org/articles/PMC9017314/
Publikováno v:
Biochemistry
The Aer2 receptor from Pseudomonas aeruginosa has an O(2)-binding PAS-heme domain that stabilizes O(2) via a Trp residue in the distal heme pocket. Trp rotates ~90° to bond with ligand and initiate signaling. Although the isolated PAS domain is mono
Autor:
Michael V Airola, Nattakan Sukomon, Dipanjan Samanta, Peter P Borbat, Jack H Freed, Kylie J Watts, Brian R Crane
Publikováno v:
PLoS Biology, Vol 11, Iss 2, p e1001479 (2013)
HAMP domains are signal relay modules in >26,000 receptors of bacteria, eukaryotes, and archaea that mediate processes involved in chemotaxis, pathogenesis, and biofilm formation. We identify two HAMP conformations distinguished by a four- to two-hel
Externí odkaz:
https://doaj.org/article/93eb518684504e138044a86d01652731
Autor:
Kylie J. Watts, Emilie Orillard
Publikováno v:
Mol Microbiol
Pseudomonas aeruginosa is an opportunistic pathogen that senses and responds to its environment via four chemosensory systems. Oxygen activates the Che2 chemosensory system by binding to the PAS-heme domain of the Aer2 receptor. Ostensibly, the outpu
Autor:
Ariane Briegel, Petra Mann, Grant J. Jensen, Sahand Pirbadian, Andreas Kjaer, Poorna Subramanian, Marina G. Kalyuzhnaya, Romain Kooger, Kylie J. Watts, Songye Chen, Simon Ringgaard, David A. Collins, Davi R. Ortega, Wen Yang
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
Nature Communications, 11 (1)
Nature Communications
Nature Communications, 11, 2041
Nature Communications, 11 (1)
Nature Communications
Nature Communications, 11, 2041
How complex, multi-component macromolecular machines evolved remains poorly understood. Here we reveal the evolutionary origins of the chemosensory machinery that controls flagellar motility in Escherichia coli. We first identify ancestral forms stil
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abaa740ff47e180a62e9ca6d4ddf1501
https://hdl.handle.net/1887/3134918
https://hdl.handle.net/1887/3134918