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6ZSX

M2 mutant (R111K:Y134F:T54V:R132Q:P39Y:R59Y) of human cellular retinoic acid binding protein II - 4 conjugate

Summary for 6ZSX
Entry DOI10.2210/pdb6zsx/pdb
Related6Z2U 6Z2Z 6ZSW
DescriptorCellular retinoic acid-binding protein 2, methyl (~{Z})-2-methyl-3-phenyl-prop-2-enoate (3 entities in total)
Functional Keywordshuman cellular retinoic acid binding protein ii, hcrabpii, conjigate, chromophore, m2, transport protein
Biological sourceHomo sapiens (Human)
Total number of polymer chains1
Total formula weight16168.48
Authors
Tassone, G.,Pozzi, C.,Mangani, S. (deposition date: 2020-07-16, release date: 2021-07-28, Last modification date: 2024-10-16)
Primary citationTassone, G.,Paolino, M.,Pozzi, C.,Reale, A.,Salvini, L.,Giorgi, G.,Orlandini, M.,Galvagni, F.,Mangani, S.,Yang, X.,Carlotti, B.,Ortica, F.,Latterini, L.,Olivucci, M.,Cappelli, A.
Xanthopsin-Like Systems via Site-Specific Click-Functionalization of a Retinoic Acid Binding Protein.
Chembiochem, 23:e202100449-e202100449, 2022
Cited by
PubMed Abstract: The use of light-responsive proteins to control both living or synthetic cells, is at the core of the expanding fields of optogenetics and synthetic biology. It is thus apparent that a richer reaction toolbox for the preparation of such systems is of fundamental importance. Here, we provide a proof-of-principle demonstration that Morita-Baylis-Hillman adducts can be employed to perform a facile site-specific, irreversible and diastereoselective click-functionalization of a lysine residue buried into a lipophilic binding pocket and yielding an unnatural chromophore with an extended π-system. In doing so we effectively open the path to the in vitro preparation of a library of synthetic proteins structurally reminiscent of xanthopsin eubacterial photoreceptors. We argue that such a library, made of variable unnatural chromophores inserted in an easy-to-mutate and crystallize retinoic acid transporter, significantly expand the scope of the recently introduced rhodopsin mimics as both optogenetic and "lab-on-a-molecule" tools.
PubMed: 34647400
DOI: 10.1002/cbic.202100449
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

226707

數據於2024-10-30公開中

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