作者: Kylie J. Watts , Barry L. Taylor , Mark S. Johnson
DOI: 10.1111/J.1365-2958.2010.07477.X
关键词: Architecture domain 、 Chemotaxis 、 PAS domain 、 Cell biology 、 Plasma protein binding 、 Biology 、 HAMP 、 Biochemistry 、 Signal transduction 、 Protein structure 、 HAMP domain
摘要: Poly-HAMP domains are widespread in bacterial chemoreceptors, but previous studies have focused on receptors with single HAMP domains. The Pseudomonas aeruginosa chemoreceptor, Aer-2, has an unusual domain architecture consisting of a PAS-sensing sandwiched between three N-terminal and two C-terminal domains, followed by conserved kinase control module. structure the was recently solved, making Aer-2 first protein resolved poly-HAMP structure. role P. is unclear, here we show that can interact chemotaxis system Escherichia coli to mediate repellent responses oxygen, carbon monoxide nitric oxide. Using this model investigate signalling function, determined PAS binds penta-co-ordinated b-type haem reversible requires four five Deleting 2 and/or 3 resulted kinase-off phenotype, whereas deleting 4 5 kinase-on phenotype. Overall, these data support which ligand-bound act together relieve inhibition module 5, resulting state receptor.