1s67

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spinqualitylabelsall models 1s67, resolution 1.5Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of heme domain of direct oxygen sensor from E. coli

Overview

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.

About this Structure

1S67 is a Single protein structure of sequence from Escherichia coli with HEM and OXY as ligands. Full crystallographic information is available from OCA.

Reference

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)., Park H, Suquet C, Satterlee JD, Kang C, Biochemistry. 2004 Mar 16;43(10):2738-46. PMID:15005609

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