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Structure-based hypothesis on the activation of the CO-sensing transcription factor CooA by Mandula Borjigin; Huiying Li; Nicholas D. Lanz; Robert L. Kerby; Gary P. Roberts; Thomas L. Poulos is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Structure-based hypothesis on the activation of the CO-sensing transcription factor CooA about?

The CooA family of proteins are prokaryotic CO-sensing transcription factors that regulate the expression of genes involved in the utilization of CO as an energy source. They are homodimeric proteins that contain two hemes. Each monomer contains an N-terminal heme-binding domain and a C-terminal DNA-binding domain. Binding of CO to the heme leads to activation by a large reorientation of the DNAbinding domain such that the DNA-binding domain is in position for specific DNA recognition. The crystal structure of CooA from Rhodospirillum rubrum [RrCooA; Lanzilotta et al. (2000), Nature Struct. Biol. 7, 876-880] in the inactive COfree off-state shows that the N-terminal Pro residue of monomer A coordinates the heme of monomer B and vice versa. It now appears that the CO replaces the Pro ligand and that this change is coupled to the activation process. However, precisely how the replacement of the Pro ligand by CO results in structural changes some 25 A ̊from the CO-binding site remains unknown. Here, the structure of a CooA variant from the thermophilic bacterium Carboxydothermus hydrogenoformans (ChCooA) is reported in which one monomer is fully in the on-state. The N-terminal region

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Author

Mandula Borjigin; Huiying Li; Nicholas D. Lanz; Robert L. Kerby; Gary P. Roberts; Thomas L. Poulos

Publisher

International Union of Crystallography; Blackwell Publishing Inc.; International Union of Crystallography (IUCr) (ISSN 0907-4449)

Published

2007

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)