4Q24
Crystal structure of Cyclo(L-leucyl-L-phenylalanyl) synthase
Summary for 4Q24
| Entry DOI | 10.2210/pdb4q24/pdb |
| Related | 3OQV |
| Descriptor | Cyclo(L-leucyl-L-phenylalanyl) synthase, PHENYLMETHYL N-[(2S)-4-CHLORO-3-OXO-1-PHENYL-BUTAN-2-YL]CARBAMATE (3 entities in total) |
| Functional Keywords | rossmann fold, cyclodipeptide synthase, aminoacyl-trna, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
| Biological source | Streptomyces noursei |
| Total number of polymer chains | 1 |
| Total formula weight | 28233.24 |
| Authors | Moutiez, M.,Schmitt, E.,Seguin, J.,Thai, R.,Favry, E.,Mechulam, Y.,Gondry, M. (deposition date: 2014-04-07, release date: 2014-10-08, Last modification date: 2024-12-25) |
| Primary citation | Moutiez, M.,Schmitt, E.,Seguin, J.,Thai, R.,Favry, E.,Belin, P.,Mechulam, Y.,Gondry, M. Unravelling the mechanism of non-ribosomal peptide synthesis by cyclodipeptide synthases. Nat Commun, 5:5141-5141, 2014 Cited by PubMed Abstract: Cyclodipeptide synthases form cyclodipeptides from two aminoacyl transfer RNAs. They use a ping-pong mechanism that begins with transfer of the aminoacyl moiety of the first aminoacyl tRNA onto a conserved serine, yielding an aminoacyl enzyme. Combining X-ray crystallography, site-directed mutagenesis and affinity labelling of the cyclodipeptide synthase AlbC, we demonstrate that the covalent intermediate reacts with the aminoacyl moiety of the second aminoacyl tRNA, forming a dipeptidyl enzyme, and identify the aminoacyl-binding sites of the aminoacyl tRNAs. PubMed: 25284085DOI: 10.1038/ncomms6141 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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