3ZOF

Crystal structure of FMN-binding protein (YP_005476) from Thermus thermophilus with bound benzene-1,4-diol

Summary for 3ZOF

• Entry DOI: 10.2210/pdb3zof/pdb
• Related: 3ZOC 3ZOD 3ZOE
• Descriptor: FLAVOREDOXIN, benzene-1,4-diol, FLAVIN MONONUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: fmn-binding protein
• Biological source: THERMUS THERMOPHILUS
• Total number of polymer chains: 2
• Total formula weight: 40615.79

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

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: 24954722
DOI: 10.1038/NCOMMS5150

Experimental method

X-RAY DIFFRACTION (2.15 Å)