title: Structural basis for oxygen sensing and signal transduction of the heme-based sensor protein Aer2 from Pseudomonas aeruginosa.
abstract: The crystal structure of a truncated Aer2, a signal transducer protein from Pseudomonas aeruginosa, consisting of the heme-containing PAS and di-HAMP domains revealed that a distal tryptophan residue (Trp283) plays an important role in stabilizing the heme-bound O(2) and intra-molecular signal transduction upon O(2) binding.
authors.affiliation: Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki 444-8787, Japan.
authors.forename: Hitomi
authors.initials: H
authors.lastname: Sawai
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Sugimoto
authors.forename: Yoshitsugu
authors.initials: Y
authors.lastname: Shiro
authors.forename: Haruto
authors.initials: H
authors.lastname: Ishikawa
authors.forename: Yasuhisa
authors.initials: Y
authors.lastname: Mizutani
authors.forename: Shigetoshi
authors.initials: S
authors.lastname: Aono
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D006420:Hemeproteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010100:Oxygen / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D011550:Pseudomonas aeruginosa / Q000737:chemistry* / Q000378:metabolism; D015398:Signal Transduction
chemical_list: D001426:Bacterial Proteins; D006420:Hemeproteins; D010100:Oxygen