Crystallization (Comment) | Organism |
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structural characterization of the oxygen-sensing globin domain, the middle domain and the catalytic GGDEF omain in apo and substrate-bound forms. The structural changes between the iron(III) and iron(II) forms of the sensor globin domain suggest a mechanism for oxygen-dependent regulation. Enzyme forms a constitutive dimer and in this form its enzymatic activity is regulated by oxygen binding. The middle domain of DosC connects the sensory and effector modules and is likely to be both essential for and directly involved in the intramolecular signal transduction in DosC | Escherichia coli |
Organism | UniProt | Comment | Textmining |
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Escherichia coli | P0AA89 | - |
- |
Synonyms | Comment | Organism |
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DosC | - |
Escherichia coli |