6asv | pdb_00006asv

E. coli PRPP Synthetase

spinqualitylabelsall models 6asv, resolution 2.21Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6asv is a 3 chain structure with sequence from Eco57. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, PO4 Gene: prs, prsA, Z1978, ECs1712 (ECO57) Activity: Ribose-phosphate diphosphokinase, with EC number 2.7.6.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [KPRS_ECO57] Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).[HAMAP-Rule:MF_00583] Publication Abstract from PubMed BACKGROUND: Ribose-phosphate pyrophosphokinase (EC 2.7.6.1) is an enzyme that catalyzes the ATP-dependent conversion of ribose-5-phosphate to phosphoribosyl pyrophosphate. The reaction product is a key precursor for the biosynthesis of purine and pyrimidine nucleotides. RESULTS: We report the 2.2 A crystal structure of the E. coli ribose-phosphate pyrophosphobinase (EcKPRS). The protein has two type I phosphoribosyltransferase folds, related by 2-fold pseudosymmetry. The propeller-shaped homohexameric structure of KPRS is composed of a trimer of dimers, with the C-terminal domains forming the dimeric blades of the propeller and the N-terminal domains forming the hexameric core. The key, conserved active site residues are well-defined in the structure and positioned appropriately to bind substrates, adenosine monophosphate and ribose-5-phosphate. The allosteric site is also relatively well conserved but, in the EcKPRS structure, several residues from a flexible loop occupy the site where the allosteric modulator, adenosine diphosphate, is predicted to bind. The presence of the loop in the allosteric site may be an additional level of regulation, whereby low affinity molecules are precluded from binding. CONCLUSIONS: Overall, this study details key structural features of an enzyme that catalyzes a critical step in nucleotide metabolism. This work provides a framework for future studies of this important protein and, as nucleotides are critical for viability, may serve as a foundation for the development of novel anti-bacterial drugs. Crystal structure of E. coli PRPP synthetase.,Zhou W, Tsai A, Dattmore DA, Stives DP, Chitrakar I, D'alessandro AM, Patil S, Hicks KA, French JB BMC Struct Biol. 2019 Jan 15;19(1):1. doi: 10.1186/s12900-019-0100-4. PMID:30646888 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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