5mlq | pdb_00005mlq

Structure of CDPS from Nocardia brasiliensis

spinqualitylabelsall models 5mlq, resolution 3.18Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5mlq is a 2 chain structure with sequence from Nocardia brasiliensis ATCC 700358. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.18Å Ligands: CIT, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function K0F6G5_NOCBR Publication Abstract from PubMed 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. Structural basis for partition of the cyclodipeptide synthases into two subfamilies.,Bourgeois G, Seguin J, Babin M, Belin P, Moutiez M, Mechulam Y, Gondry M, Schmitt E J Struct Biol. 2018 Jul;203(1):17-26. doi: 10.1016/j.jsb.2018.03.001. Epub 2018, Mar 2. PMID:29505829 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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