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6PO6

MicroED Structure of a Natural Product VFAThiaGlu

Summary for 6PO6
Entry DOI10.2210/pdb6po6/pdb
EMDB information20411
DescriptorYFAThiaGlu (2 entities in total)
Functional Keywordsribosomal synthesized small peptide, microed, microcrystal electron diffraction, unknown function
Biological sourcePseudomonas syringae
Total number of polymer chains1
Total formula weight482.55
Authors
Halaby, S.,Gonen, T.,Ting, C.P.,Funk, M.A.,van der Donk, W.A. (deposition date: 2019-07-03, release date: 2019-08-07, Last modification date: 2023-11-15)
Primary citationTing, C.P.,Funk, M.A.,Halaby, S.L.,Zhang, Z.,Gonen, T.,van der Donk, W.A.
Use of a scaffold peptide in the biosynthesis of amino acid-derived natural products.
Science, 365:280-284, 2019
Cited by
PubMed Abstract: Genome sequencing of environmental bacteria allows identification of biosynthetic gene clusters encoding unusual combinations of enzymes that produce unknown natural products. We identified a pathway in which a ribosomally synthesized small peptide serves as a scaffold for nonribosomal peptide extension and chemical modification. Amino acids are transferred to the carboxyl terminus of the peptide through adenosine triphosphate and amino acyl-tRNA-dependent chemistry that is independent of the ribosome. Oxidative rearrangement, carboxymethylation, and proteolysis of a terminal cysteine yields an amino acid-derived small molecule. Microcrystal electron diffraction demonstrates that the resulting product is isosteric to glutamate. We show that a similar peptide extension is used during the biosynthesis of the ammosamides, which are cytotoxic pyrroloquinoline alkaloids. These results suggest an alternative paradigm for biosynthesis of amino acid-derived natural products.
PubMed: 31320540
DOI: 10.1126/science.aau6232
PDB entries with the same primary citation
Experimental method
ELECTRON CRYSTALLOGRAPHY (1 Å)
Structure validation

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