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8J2X

Saccharothrix syringae photocobilins protein, light state

Summary for 8J2X
Entry DOI10.2210/pdb8j2x/pdb
DescriptorCobalamin-binding protein, COBALAMIN, BILIVERDINE IX ALPHA, ... (5 entities in total)
Functional Keywordscobalamin binding, biliverdin binding, b12-dependent photoreceptor protein, photocobilins, unknown function
Biological sourceSaccharothrix syringae
Total number of polymer chains1
Total formula weight38426.29
Authors
Zhang, S.,Poddar, H.,Levy, C.,Leys, D. (deposition date: 2023-04-15, release date: 2024-04-10)
Primary citationZhang, 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: 38548733
DOI: 10.1038/s41467-024-46995-1
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.98 Å)
Structure validation

237735

数据于2025-06-18公开中

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