Interplay between chromophore binding and domain assembly by the B12-dependent photoreceptor protein, CarH
0301 basic medicine
Chemistry
03 medical and health sciences
ResearchInstitutes_Networks_Beacons/manchester_institute_of_biotechnology; name=Manchester Institute of Biotechnology
612
ResearchInstitutes_Networks_Beacons/photon_science_institute; name=Photon Science Institute
DOI:
10.1039/d1sc00522g
Publication Date:
2021-05-06T04:42:55Z
AUTHORS (9)
ABSTRACT
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.
SUPPLEMENTAL MATERIAL
Coming soon ....
REFERENCES (25)
CITATIONS (12)
EXTERNAL LINKS
PlumX Metrics
RECOMMENDATIONS
FAIR ASSESSMENT
Coming soon ....
JUPYTER LAB
Coming soon ....