A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation by M. F. Symmons and others 2026-11-05
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M. F. Symmons, G. H. Jones, B. F. Luisi; Structure8(11),1215–1226(2000), DOI10.1016/S0969-2126(00)00521-9. Publisher primary abstract www.sciencedirect.com/science/article/pii/S0969212600005219 : X-ray structure of Streptomyces antibioticus PNPase without bound RNA but with tungstate at catalytic sites, trimer and central channel. A possible channel role in processivity is proposed, not direct observation of RNA transit. No initials expanded.
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Overexpression and purification of untagged polynucleotide phosphorylases by George H. Jones and others 2026-11-05
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Verified locator: Protein Expr Purif32(2),202–209(2003), DOI10.1016/j.pep.2003.08.005. Full bylines George H Jones and Martyn F Symmons; Abstract: purified bacterial PNPases tested for polymerization/phosphorolysis and phosphate-independent nuclease contamination.
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