5t3o

Crystal structure of the Phosphorybosylpyrophosphate synthetase II from Thermus thermophilus

spinqualitylabelsall models 5t3o, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5t3o is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, SO4 Activity: Ribose-phosphate diphosphokinase, with EC number 2.7.6.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [Q5SHU3_THET8] Involved in the biosynthesis of ribose 1,5-bisphosphate. Catalyzes the transfer of pyrophosphoryl group from ATP to ribose-5-phosphate to yield phosphoribosyl diphosphate (PRPP) and AMP.[HAMAP-Rule:MF_00583] Publication Abstract from PubMed Phosphoribosylpyrophosphate synthetase (PRPPS) from the thermophilic bacterial strain Thermus thermophilus HB27 catalyzes the synthesis of phosphoribosylpyrophosphate from ribose 5-phosphate and ATP, and belongs to the class I PRPPSs. The three-dimensional structure of the recombinant enzyme was solved at 2.2 A resolution using crystals grown in microgravity from protein solution containing ATP, magnesium and sulfate ions. An ADP molecule was located in the active site of each subunit of the hexameric enzyme molecule and sulfate ions were located in both the active and allosteric sites. It was found that the catalytic loop that restricts the active-site area and is usually missing from the electron-density map of class I PRPPSs adopts different conformations in three independent subunits in T. thermophilus PRPPS. A closed conformation of the active site was found in one of subunits where the highly ordered catalytic beta-hairpin delivers the Lys and Arg residues that are essential for activity directly to the ADP molecule, which occupies the ATP-binding site. A comparison of the conformations of the catalytic loop in the three independent subunits reveals a possible mode of transition from the open to the closed state of the active site during the course of the catalyzed reaction. Crystal structure of recombinant phosphoribosylpyrophosphate synthetase 2 from Thermus thermophilus HB27 complexed with ADP and sulfate ions.,Timofeev VI, Sinitsyna EV, Kostromina MA, Muravieva TI, Makarov DA, Mikheeva OO, Kuranova IP, Esipov RS Acta Crystallogr F Struct Biol Commun. 2017 Jun 1;73(Pt 6):369-375. doi:, 10.1107/S2053230X17007488. Epub 2017 May 31. PMID:28580926 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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