3ZOH
Crystal structure of FMN-binding protein (YP_005476) from Thermus thermophilus with bound 1-Cyclohex-2-enone
Summary for 3ZOH
| Entry DOI | 10.2210/pdb3zoh/pdb |
| Related | 3ZOC 3ZOD 3ZOE 3ZOF 3ZOG |
| Descriptor | FLAVOREDOXIN, cyclohex-2-en-1-one, FLAVIN MONONUCLEOTIDE, ... (4 entities in total) |
| Functional Keywords | fmn-binding protein, cyclohexenone |
| Biological source | THERMUS THERMOPHILUS |
| Total number of polymer chains | 4 |
| Total formula weight | 81175.64 |
| Authors | Pavkov-Keller, T.,Steinkellner, G.,Gruber, C.C.,Steiner, K.,Winkler, C.,Schwamberger, O.,Schwab, H.,Faber, K.,Gruber, K. (deposition date: 2013-02-21, release date: 2014-05-14, Last modification date: 2023-12-20) |
| Primary citation | Steinkellner, G.,Gruber, C.C.,Pavkov-Keller, T.,Binter, A.,Steiner, K.,Winkler, C.,Lyskowski, A.,Schwamberger, O.,Oberer, M.,Schwab, H.,Faber, K.,Macheroux, P.,Gruber, K. Identification of Promiscuous Ene-Reductase Activity by Mining Structural Databases Using Active Site Constellations. Nat.Commun., 5:4150-, 2014 Cited by PubMed Abstract: The exploitation of catalytic promiscuity and the application of de novo design have recently opened the access to novel, non-natural enzymatic activities. Here we describe a structural bioinformatic method for predicting catalytic activities of enzymes based on three-dimensional constellations of functional groups in active sites ('catalophores'). As a proof-of-concept we identify two enzymes with predicted promiscuous ene-reductase activity (reduction of activated C-C double bonds) and compare them with known ene-reductases, that is, members of the Old Yellow Enzyme family. Despite completely different amino acid sequences, overall structures and protein folds, high-resolution crystal structures reveal equivalent binding modes of typical Old Yellow Enzyme substrates and ligands. Biochemical and biocatalytic data show that the two enzymes indeed possess ene-reductase activity and reveal an inverted stereopreference compared with Old Yellow Enzymes for some substrates. This method could thus be a tool for the identification of viable starting points for the development and engineering of novel biocatalysts. PubMed: 24954722DOI: 10.1038/NCOMMS5150 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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