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 Å using Fe multiple-wavelength anomalous dispersion (MAD), and the positions of Met95 have been confirmed by selenomethionine (SeMet) MAD. Ec DosH is the sensing part of a large...

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Veröffentlicht in:	Biochemistry (Easton) 2004-03, Vol.43 (10), p.2738-2746
Hauptverfasser:	Park, Suquet, Christine, Satterlee, James D, Kang, ChulHee
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Aryl Hydrocarbon Receptor Nuclear Translocator Bacterial Proteins - chemistry Bradyrhizobium - chemistry Carrier Proteins - chemistry Carrier Proteins - physiology Crystallography, X-Ray Dimerization DNA-Binding Proteins Escherichia coli Escherichia coli Proteins - chemistry Escherichia coli Proteins - physiology Heme - chemistry Hemeproteins - chemistry Hemeproteins - physiology Ligands Molecular Sequence Data Oxygen - chemistry Phosphoric Diester Hydrolases Protein Structure, Tertiary - physiology Receptors, Aryl Hydrocarbon - chemistry Receptors, Aryl Hydrocarbon - physiology Recombinant Proteins - chemistry Sequence Alignment Signal Transduction Transcription Factors - chemistry Transcription Factors - physiology
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