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PDBsum entry 1s67
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Oxygen storage/transport
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PDB id
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1s67
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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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).
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Authors
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H.Park,
C.Suquet,
J.D.Satterlee,
C.Kang.
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Ref.
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Biochemistry, 2004,
43,
2738-2746.
[DOI no: ]
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PubMed id
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Abstract
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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.
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