The structure of a pyrophosphate-dependent phosphofructokinase from the lyme disease spirochete Borrelia burgdorferi

Stanley A. Moore, Ron S. Ronimus, Russel S. Roberson, Hugh W. Morgan

Research output: Contribution to journalArticlepeer-review

26 Scopus citations

Abstract

The structure of the 60 kDa pyrophosphate (PPi)-dependent phosphofructokinase (PFK) from Borrelia burgdorferi has been solved and refined (Rfree = 0.243) at 2.55 Å resolution. The domain structure of eubacterial ATP-dependent PFKs is conserved in B. burgdorferi PFK, and there are three large insertions relative to E. coli PFK, including a helical domain containing a hairpin structure that interacts with the active site. Asp177, conserved in all PPi PFKs, negates the binding of the α-phosphate group of ATP and likely contacts the essential Mg2+ cation via a water molecule. Asn181 blocks the binding of the adenine moiety of ATP. Lys203 hydrogen bonds to a sulfate anion that likely mimics PPi substrate binding.

Original languageEnglish (US)
Pages (from-to)659-671
Number of pages13
JournalStructure
Volume10
Issue number5
DOIs
StatePublished - 2002

Keywords

  • Borrelia
  • Crystallography
  • Drug
  • Glycolysis
  • Phosphofructokinase
  • Pyrophosphate

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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