2004
DOI: 10.1021/bi035980p
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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)

Abstract: 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 mo… Show more

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Cited by 124 publications
(246 citation statements)
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“…The three-dimensional structures of the Fe(III), Fe(II), and Fe(II)-O 2 complexes of the isolated heme sensor domain of EcDosH (EcDosH) have been determined (7,8). These structures have revealed the importance of several key amino acids near the distal heme-binding site involved in changes in the heme environment upon O 2 binding.…”
Section: Dos From Escherichia Coli (Ecdos)mentioning
confidence: 99%
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“…The three-dimensional structures of the Fe(III), Fe(II), and Fe(II)-O 2 complexes of the isolated heme sensor domain of EcDosH (EcDosH) have been determined (7,8). These structures have revealed the importance of several key amino acids near the distal heme-binding site involved in changes in the heme environment upon O 2 binding.…”
Section: Dos From Escherichia Coli (Ecdos)mentioning
confidence: 99%
“…The heme sensor domain EcDosH crystallizes as a dimer (7,8) and is also dimeric in solution (1). Surprisingly, based on gel filtration chromatography, full-length EcDos has been characterized as a tetramer (12,13).…”
Section: Dos From Escherichia Coli (Ecdos)mentioning
confidence: 99%
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