7YK1

Structural basis of human PRPS2 filaments

Summary for 7YK1

• Entry DOI: 10.2210/pdb7yk1/pdb
• EMDB information: 33883
• Descriptor: Ribose-phosphate pyrophosphokinase 2, PHOSPHATE ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: phosphoribosylpyrophosphate synthetase, complex, filament, transferase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 6
• Total formula weight: 219687.88

Authors

Lu, G.M.,Hu, H.H.,Liu, J.L. (deposition date: 2022-07-21, release date: 2023-08-02, Last modification date: 2025-09-17)

Primary citation

Lu, G.M.,Hu, H.H.,Chang, C.C.,Zhong, J.,Zhou, X.,Guo, C.J.,Zhang, T.,Li, Y.L.,Yin, B.,Liu, J.L.
Structural basis of human PRPS2 filaments.
Cell Biosci, 13:100-100, 2023

PubMed Abstract: PRPP synthase (PRPS) transfers the pyrophosphate groups from ATP to ribose-5-phosphate to produce 5-phosphate ribose-1-pyrophosphate (PRPP), a key intermediate in the biosynthesis of several metabolites including nucleotides, dinucleotides and some amino acids. There are three PRPS isoforms encoded in human genome. While human PRPS1 (hPRPS1) and human PRPS2 (hPRPS2) are expressed in most tissues, human PRPS3 (hPRPS3) is exclusively expressed in testis. Although hPRPS1 and hPRPS2 share 95% sequence identity, hPRPS2 has been shown to be less sensitive to allosteric inhibition and specifically upregulated in certain cancers in the translational level. Recent studies demonstrate that PRPS can form a subcellular compartment termed the cytoophidium in multiple organisms across prokaryotes and eukaryotes. Forming filaments and cytoophidia is considered as a distinctive mechanism involving the polymerization of the protein. Previously we solved the filament structures of Escherichia coli PRPS (ecPRPS) using cryo-electron microscopy (cryo-EM) .

PubMed: 37248548
DOI: 10.1186/s13578-023-01037-z

Experimental method

ELECTRON MICROSCOPY (3.08 Å)