Interplay between chromophore binding and domain assembly by the B12-dependent photoreceptor protein, CarH

• DOI: 10.1039/d1sc00522g
• Publication Date: 2021-05-06T04:42:55Z
• Authors: Inês S. Camacho; Rachelle Black; Derren J. Heyes; Linus O. Johannissen; Lennart A. I. Ram...; Bruno Bellina; Perdita E. Barran; Sam Hay; Alex R. Jones
• Keywords: 0301 basic medicine; Chemistry; 0303 health sciences; 03 medical and health sciences; 13. Climate action; ResearchInstitutes_Networks_Beacons/manchester_institute_of_biotechnology; name=Manchester Institute of Biotechnology; 612; ResearchInstitutes_Networks_Beacons/photon_science_institute; name=Photon Science Institute; 7. Clean energy

The function of the bacterial photoreceptor protein, CarH, is regulated by changes to its oligomeric state. Camacho et al. detail how binding of vitamin B12 in the dark drives assembly of the protein tetramer that in turn blocks transcription.