6ULX
Adenylation domain of a keto acid-selecting NRPS module bound to keto acyl adenylate space group P43212
Summary for 6ULX
| Entry DOI | 10.2210/pdb6ulx/pdb |
| Descriptor | Amino acid adenylation domain-containing protein, 5'-O-{(S)-hydroxy[(4-methyl-2-oxopentanoyl)oxy]phosphoryl}adenosine, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | nrps, nonribosomal peptide synthetase, non-ribosomal peptide synthetase, adenylation, adenylation domain, depsipeptide, cereulide, valinomycin, natural product, adenylate, keto acid, ketoacid, biosynthetic protein |
| Biological source | Bacillus stratosphericus LAMA 585 |
| Total number of polymer chains | 1 |
| Total formula weight | 66028.77 |
| Authors | Alonzo, D.A.,Chiche-Lapierre, C.,Schmeing, T.M. (deposition date: 2019-10-08, release date: 2020-02-19, Last modification date: 2024-03-13) |
| Primary citation | Alonzo, D.A.,Chiche-Lapierre, C.,Tarry, M.J.,Wang, J.,Schmeing, T.M. Structural basis of keto acid utilization in nonribosomal depsipeptide synthesis. Nat.Chem.Biol., 16:493-496, 2020 Cited by PubMed Abstract: Nonribosomal depsipeptides are natural products composed of amino and hydroxy acid residues. The hydroxy acid residues often derive from α-keto acids, reduced by ketoreductase domains in the depsipeptide synthetases. Biochemistry and structures reveal the mechanism of discrimination for α-keto acids and a remarkable architecture: flanking intact adenylation and ketoreductase domains are sequences separated by >1,100 residues that form a split 'pseudoA' domain, structurally important for the depsipeptide module's synthetic cycle. PubMed: 32066969DOI: 10.1038/s41589-020-0481-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.31 Å) |
Structure validation
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