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7QCW

Apo-structure of serine hydroxymethyltransferase (PbzB) involved in benzobactin biosynthesis in P. chlororaphis subsp. piscium DSM 21509

Summary for 7QCW
Entry DOI10.2210/pdb7qcw/pdb
DescriptorSerine hydroxymethyltransferase (1 entity in total)
Functional Keywordsnatural product biosynthesis, benzobactin, serine hydroxymethyltransferase, benzoxazolinate, biosynthetic protein
Biological sourcePseudomonas chlororaphis subsp. piscium
Total number of polymer chains2
Total formula weight98914.42
Authors
Czech, L.,Bange, G. (deposition date: 2021-11-25, release date: 2022-10-12, Last modification date: 2024-01-31)
Primary citationShi, 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: 36198080
DOI: 10.1002/anie.202206106
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.81 Å)
Structure validation

226707

数据于2024-10-30公开中

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