6Z2U
M2 mutant (R111K:Y134F:T54V:R132Q:P39Y:R59Y) of human cellular retinoic acid binding protein II
Summary for 6Z2U
| Entry DOI | 10.2210/pdb6z2u/pdb |
| Descriptor | Cellular retinoic acid-binding protein 2 (2 entities in total) |
| Functional Keywords | human cellular retinoic acid binding protein ii, hcrabpii, m2, transport protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 15992.26 |
| Authors | Tassone, G.,Pozzi, C.,Mangani, S. (deposition date: 2020-05-18, release date: 2021-06-02, Last modification date: 2024-01-24) |
| Primary citation | Tassone, 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: 34647400DOI: 10.1002/cbic.202100449 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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