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.

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.

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Crystallography, X-Ray
  • Hemeproteins / chemistry*
  • Hemeproteins / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Oxygen / metabolism*
  • Protein Structure, Tertiary
  • Pseudomonas aeruginosa / chemistry*
  • Pseudomonas aeruginosa / metabolism
  • Signal Transduction

Substances

  • Bacterial Proteins
  • Hemeproteins
  • Oxygen