7QCW
Apo-structure of serine hydroxymethyltransferase (PbzB) involved in benzobactin biosynthesis in P. chlororaphis subsp. piscium DSM 21509
Summary for 7QCW
Entry DOI | 10.2210/pdb7qcw/pdb |
Descriptor | Serine hydroxymethyltransferase (1 entity in total) |
Functional Keywords | natural product biosynthesis, benzobactin, serine hydroxymethyltransferase, benzoxazolinate, biosynthetic protein |
Biological source | Pseudomonas chlororaphis subsp. piscium |
Total number of polymer chains | 2 |
Total formula weight | 98914.42 |
Authors | |
Primary citation | Shi, Y.M.,Crames, J.J.,Czech, L.,Bozhuyuk, K.A.J.,Shi, Y.N.,Hirschmann, M.,Lamberth, S.,Claus, P.,Paczia, N.,Ruckert, C.,Kalinowski, J.,Bange, G.,Bode, H.B. Genome Mining Enabled by Biosynthetic Characterization Uncovers a Class of Benzoxazolinate-Containing Natural Products in Diverse Bacteria. Angew.Chem.Int.Ed.Engl., 61:e202206106-e202206106, 2022 Cited by PubMed Abstract: Benzoxazolinate is a rare bis-heterocyclic moiety that interacts with proteins and DNA and confers extraordinary bioactivities on natural products, such as C-1027. However, the biosynthetic gene responsible for the key cyclization step of benzoxazolinate remains unclear. Herein, we show a putative acyl AMP-ligase responsible for the last cyclization step. We used the enzyme as a probe for genome mining and discovered that the orphan benzobactin gene cluster in entomopathogenic bacteria prevails across Proteobacteria and Firmicutes. It turns out that Pseudomonas chlororaphis produces various benzobactins, whose biosynthesis is highlighted by a synergistic effect of two unclustered genes encoding enzymes on boosting benzobactin production; the formation of non-proteinogenic 2-hydroxymethylserine by a serine hydroxymethyltransferase; and the types I and II NRPS architecture for structural diversity. Our findings reveal the biosynthetic potential of a widespread benzobactin gene cluster. PubMed: 36198080DOI: 10.1002/anie.202206106 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.81 Å) |
Structure validation
Download full validation report