6ztu

Crystal structure of a cyclodipeptide synthase from Bacillus thermoamylovorans

spinqualitylabelsall models 6ztu, resolution 1.69Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ztu is a 1 chain structure with sequence from Caldibacillus thermoamylovorans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.69Å Ligands: 0RE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A090KS30_9BACI Publication Abstract from PubMed Cyclodipeptide synthases (CDPSs) produce a variety of cyclic dipeptide products by utilising two aminoacylated tRNA substrates. We sought to investigate the minimal requirements for substrate usage in this class of enzymes as the relationship between CDPSs and their substrates remains elusive. Here, we investigated the Bacillus thermoamylovorans enzyme, BtCDPS, which synthesises cyclo(l-Leu-l-Leu). We systematically tested where specificity arises and, in the process, uncovered small molecules (activated amino esters) that will suffice as substrates, although catalytically poor. We solved the structure of BtCDPS to 1.7 A and combining crystallography, enzymatic assays and substrate docking experiments propose a model for how the minimal substrates interact with the enzyme. This work is the first report of a CDPS enzyme utilizing a molecule other than aa-tRNA as a substrate; providing insights into substrate requirements and setting the stage for the design of improved simpler substrates. Bypassing the requirement for aminoacyl-tRNA by a cyclodipeptide synthase enzyme.,Harding CJ, Sutherland E, Hanna JG, Houston DR, Czekster CM RSC Chem Biol. 2021 Jan 15;2(1):230-240. doi: 10.1039/d0cb00142b. PMID:33937777 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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