Structural highlights
Publication Abstract from PubMed
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.
Structural basis for oxygen sensing and signal transduction of the heme-based sensor protein Aer2 from Pseudomonas aeruginosa.,Sawai H, Sugimoto H, Shiro Y, Ishikawa H, Mizutani Y, Aono S Chem Commun (Camb). 2012 Jul 4;48(52):6523-5. doi: 10.1039/c2cc32549g. Epub 2012 , May 23. PMID:22622145[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sawai H, Sugimoto H, Shiro Y, Ishikawa H, Mizutani Y, Aono S. Structural basis for oxygen sensing and signal transduction of the heme-based sensor protein Aer2 from Pseudomonas aeruginosa. Chem Commun (Camb). 2012 Jul 4;48(52):6523-5. doi: 10.1039/c2cc32549g. Epub 2012 , May 23. PMID:22622145 doi:10.1039/c2cc32549g
