6PO6
MicroED Structure of a Natural Product VFAThiaGlu
Summary for 6PO6
Entry DOI | 10.2210/pdb6po6/pdb |
EMDB information | 20411 |
Descriptor | YFAThiaGlu (2 entities in total) |
Functional Keywords | ribosomal synthesized small peptide, microed, microcrystal electron diffraction, unknown function |
Biological source | Pseudomonas syringae |
Total number of polymer chains | 1 |
Total formula weight | 482.55 |
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 citation | Ting, 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: 31320540DOI: 10.1126/science.aau6232 PDB entries with the same primary citation |
Experimental method | ELECTRON CRYSTALLOGRAPHY (1 Å) |
Structure validation
Download full validation report
