Structural basis for the reversibility of proton pyrophosphatase

Kamesh C. Regmi, Gaston A. Pizzio, Roberto Gaxiola

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

Proton Pyrophosphatase (H+-PPase) is an evolutionarily conserved enzyme regarded as a bona fide vacuolar marker. However, H+-PPase also localizes at the plasma membrane of the phloem, where, evidence suggests that it functions as a Pyrophosphate Synthase and participates in phloem loading and photosynthate partitioning. We believe that this pyrophosphate synthesising function of H+-PPase is fundamentally rooted to its molecular structure, and here we postulate, on the basis of published crystal structures of membrane-bound pyrophosphatases, a plausible mechanism of pyrophosphate synthesis.

Original languageEnglish (US)
Pages (from-to)e1231294
JournalPlant signaling & behavior
Volume11
Issue number10
DOIs
StatePublished - Oct 2 2016

Keywords

  • Crystal structure
  • Proton pyrophosphatase
  • Pyrophosphate synthase
  • Sodium pyrophosphatase
  • Sodium/Proton pyrophosphatase

ASJC Scopus subject areas

  • Plant Science

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