The preferred aerobic metabolism of Pseudomonas aeruginosa requires respiratory enzymes that need iron or iron-containing cofactors for their function. The extremely low concentrations of free iron in mammalian hosts trigger a stress response in the opportunistic P. aeruginosa (and in many other pathogens) that involves the deployment of several iron-acquisition systems. The systems involved in the capture of iron typically fall in two categories, (i) excretion of low-molecular weight iron ligands (siderophores) and the receptors that take in iron-loaded siderophores through the outer membrane and (ii) direct binding of iron or iron-containing proteins at outer membrane receptors which internalize only the iron. Pseudomonas aeruginosa secretes a 205 residue long hemophore (full-length HasAp) that is subsequently cleaved at the C’-terminal domain to produce mainly a 184 residue long truncated HasAp that scavenges heme. Here you can see a recent structure of HasAp protein in complex with a synthetic pseudo-heme structure (Manganese Tetraphenylporphyrin) (PDB code: 7EMU)
#molecularart ... #immolecular ... #scavenger ... #pseudomonas ... #heme ... #iron ... #transport ... #xray
Heme-scavenging protein structure rendered with @proteinimaging and depicted with @corelphotopaint
#molecularart ... #immolecular ... #scavenger ... #pseudomonas ... #heme ... #iron ... #transport ... #xray
Heme-scavenging protein structure rendered with @proteinimaging and depicted with @corelphotopaint
