8J2X
Saccharothrix syringae photocobilins protein, light state
Summary for 8J2X
Entry DOI | 10.2210/pdb8j2x/pdb |
Descriptor | Cobalamin-binding protein, COBALAMIN, BILIVERDINE IX ALPHA, ... (5 entities in total) |
Functional Keywords | cobalamin binding, biliverdin binding, b12-dependent photoreceptor protein, photocobilins, unknown function |
Biological source | Saccharothrix syringae |
Total number of polymer chains | 1 |
Total formula weight | 38426.29 |
Authors | |
Primary citation | Zhang, S.,Jeffreys, L.N.,Poddar, H.,Yu, Y.,Liu, C.,Patel, K.,Johannissen, L.O.,Zhu, L.,Cliff, M.J.,Yan, C.,Schiro, G.,Weik, M.,Sakuma, M.,Levy, C.W.,Leys, D.,Heyes, D.J.,Scrutton, N.S. Photocobilins integrate B12 and bilin photochemistry for enzyme control. Nat Commun, 15:2740-2740, 2024 Cited by PubMed Abstract: Photoreceptor proteins utilise chromophores to sense light and trigger a biological response. The discovery that adenosylcobalamin (or coenzyme B) can act as a light-sensing chromophore heralded a new field of B-photobiology. Although microbial genome analysis indicates that photoactive B-binding domains form part of more complex protein architectures, regulating a range of molecular-cellular functions in response to light, experimental evidence is lacking. Here we identify and characterise a sub-family of multi-centre photoreceptors, termed photocobilins, that use B and biliverdin (BV) to sense light across the visible spectrum. Crystal structures reveal close juxtaposition of the B and BV chromophores, an arrangement that facilitates optical coupling. Light-triggered conversion of the B affects quaternary structure, in turn leading to light-activation of associated enzyme domains. The apparent widespread nature of photocobilins implies involvement in light regulation of a wider array of biochemical processes, and thus expands the scope for B photobiology. Their characterisation provides inspiration for the design of broad-spectrum optogenetic tools and next generation bio-photocatalysts. PubMed: 38548733DOI: 10.1038/s41467-024-46995-1 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.98 Å) |
Structure validation
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