8jfs | pdb_00008jfs

Phosphate bound acylphosphatase from Deinococcus radiodurans at 1 Angstrom resolution

spinqualitylabelsall models 8jfs, resolution 1.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8jfs is a 2 chain structure with sequence from Deinococcus radiodurans R1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1Å Ligands: CIT, EDO, NA, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ACYP_DEIRA Publication Abstract from PubMed Acylphosphatase (Acp) is a hydrolase which specifically cleaves carboxyl-phosphate bond of intermediates of metabolic pathways. It is a small cytosolic enzyme found in both prokaryotic and eukaryotic organisms. Previous crystal structures of acylphosphatase from different organisms have provided insights into the active site but the complete understanding of substrate binding and catalytic mechanisms in acylphosphatase remain elusive. Here we report the crystal structure of phosphate bound acylphosphatase from a mesothermic bacterium, Deinococcus radiodurans (drAcp) at resolution of 1.0 A. Our structural analysis shows how the terminal phosphate group of substrates is bound to the active site, highlighting the importance of arginine in substrate recognition, role of asparagine in mode of catalysis and shedding light on the reaction mechanism. Additionally, the protein can refold after thermal melting by gradually lowering the temperature. To further explore the dynamics of drAcp, molecular dynamics simulation of drAcp and homologs from thermophilic organisms were carried out which revealed similar root mean square fluctuation profile but drAcp showed comparatively higher fluctuations. Crystal structure of phosphate bound Acyl phosphatase mini-enzyme from Deinococcus radiodurans at 1A resolution.,Khakerwala Z, Kumar A, Makde RD Biochem Biophys Res Commun. 2023 Sep 3;671:153-159. doi: , 10.1016/j.bbrc.2023.06.003. Epub 2023 Jun 5. PMID:37302289 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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