Gas Sensing and Signaling in the PAS-Heme Domain of the Pseudomonas aeruginosa Aer2 Receptor.

ABSTRACT: The Aer2 chemoreceptor from Pseudomonas aeruginosa contains a PAS sensing domain that coordinates b-type heme and signals in response to the binding of O₂, CO, or NO. PAS-heme structures suggest that Aer2 uniquely coordinates heme via a His residue on a 3₁₀ helix (H234 on Eη), stabilizes O₂ binding via a Trp residue (W283), and signals via both W283 and an adjacent Leu residue (L264). Ligand binding may displace L264 and reorient W283 for hydrogen bonding to the ligand. Here, we clarified the mechanisms by which Aer2-PAS binds heme, regulates ligand binding, and initiates conformational signaling. H234 coordinated heme, but additional hydrophobic residues in the heme cleft were also critical for stable heme binding. O₂ appeared to b

SUBMITTER: Garcia D 

PROVIDER: S-EPMC5573068 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature