Insights into signal transduction involving PAS domain oxygen-sensing heme proteins from the X-ray crystal structure of Escherichia coli Dos heme domain (Ec DosH).
The X-ray crystal structure of the Escherichia coli (Ec) direct oxygen sensor heme domain (Ec DosH) has been solved to 1.8 A using Fe multiple-wavelength anomalous dispersion (MAD), and the positions of Met95 have been confirmed by selenomethionine ((Se)Met) MAD. Ec DosH is the sensing part of a larger two-domain sensing/signaling protein, in which the signaling domain has phosphodiesterase activity. The asymmetric unit of the crystal lattice contains a dimer comprised of two differently ligated heme domain monomers. Except for the heme ligands, the monomer heme domains are identical. In one monomer, the heme is ligated by molecular oxygen (O(2)), while in the other monomer, an endogenous Met95 with S --> Fe ligation replaces the exogenous O(2) ligand. In both heme domains, the proximal ligand is His77. Analysis of these structures reveals sizable ligand-dependent conformational changes in the protein chain localized in the FG turn, the G(beta)-strand, and the HI turn. These changes provide insight to the mechanism of signal propagation within the heme domain following initiation due to O(2) dissociation.
School of Molecular Biosciences, Washington State University, Pullman, Washington 99164-4660, USA.
HaJeung
H
Park
Christine
C
Suquet
James D
JD
Satterlee
ChulHee
C
Kang
D000595:Amino Acid Sequence; D051784:Aryl Hydrocarbon Receptor Nuclear Translocator; D001426:Bacterial Proteins / Q000737:chemistry; D020369:Bradyrhizobium / Q000737:chemistry; D002352:Carrier Proteins / Q000737:chemistry* / Q000502:physiology*; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins; D019281:Dimerization; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000502:physiology*; D006418:Heme / Q000737:chemistry; D006420:Hemeproteins / Q000737:chemistry* / Q000502:physiology*; D000071677:Histidine Kinase; D008024:Ligands; D008969:Molecular Sequence Data; D010100:Oxygen / Q000737:chemistry; D010727:Phosphoric Diester Hydrolases; D017434:Protein Structure, Tertiary / Q000502:physiology; D018336:Receptors, Aryl Hydrocarbon / Q000737:chemistry / Q000502:physiology; D011994:Recombinant Proteins / Q000737:chemistry; D016415:Sequence Alignment; D015398:Signal Transduction; D014157:Transcription Factors / Q000737:chemistry / Q000502:physiology
D001426:Bacterial Proteins; D002352:Carrier Proteins; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D006420:Hemeproteins; D008024:Ligands; D018336:Receptors, Aryl Hydrocarbon; D011994:Recombinant Proteins; D014157:Transcription Factors; D051784:Aryl Hydrocarbon Receptor Nuclear Translocator; D006418:Heme; C067929:FixL protein, Bacteria; D000071677:Histidine Kinase; D010727:Phosphoric Diester Hydrolases; C464427:dosP protein, E coli; D010100:Oxygen