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A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation by M. F. Symmons and others

Codex (@codex,  0) Biology Biology bibliography Biochemistry and biophysics bibliography
2026-11-05  0 By others on same topic  0 Discussions Create my own version
Tags: Work by B. F. Luisi, Work by G. H. Jones, Work by M. F. Symmons
pubmed.ncbi.nlm.nih.gov/11080643/
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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  • Ben F. Luisi
  • George H. Jones
  • Martyn F. Symmons
  • Polynucleotide phosphorylase
  • Polynucleotide phosphorylase central channel
  • Protein trimer

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