6EZ3
Structure of CDPS from Staphylococcus haemolyticus
Summary for 6EZ3
| Entry DOI | 10.2210/pdb6ez3/pdb |
| Related | 4q24 |
| Descriptor | Cyclo(L-leucyl-L-leucyl) synthase, SULFATE ION (3 entities in total) |
| Functional Keywords | trna, cyclodipeptide, rna binding protein |
| Biological source | Staphylococcus haemolyticus (strain JCSC1435) |
| Total number of polymer chains | 6 |
| Total formula weight | 165392.29 |
| Authors | Schmitt, E.,Mechulam, Y.,Bourgeois, G. (deposition date: 2017-11-14, release date: 2018-11-14, Last modification date: 2024-05-08) |
| Primary citation | Bourgeois, G.,Seguin, J.,Babin, M.,Belin, P.,Moutiez, M.,Mechulam, Y.,Gondry, M.,Schmitt, E. Structural basis for partition of the cyclodipeptide synthases into two subfamilies. J. Struct. Biol., 203:17-26, 2018 Cited by PubMed Abstract: Cyclodipeptide synthases (CDPSs) use two aminoacyl-tRNAs to catalyze the formation of two peptide bonds leading to cyclodipeptides that can be further used for the synthesis of diketopiperazines. It was shown that CDPSs fall into two subfamilies, NYH and XYP, characterized by the presence of specific sequence signatures. However, current understanding of CDPSs only comes from studies of enzymes from the NYH subfamily. The present study reveals the crystal structures of three CDPSs from the XYP subfamily. Comparison of the XYP and NYH enzymes shows that the two subfamilies mainly differ in the first half of their Rossmann fold. This gives a structural basis for the partition of CDPSs into two subfamilies. Despite these differences, the catalytic residues adopt similar positioning regardless of the subfamily suggesting that the XYP and NYH motifs correspond to two structural solutions to facilitate the reactivity of the catalytic serine residue. PubMed: 29505829DOI: 10.1016/j.jsb.2018.03.001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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