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Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae.

Imtiaz AliSungmin EuDaniel KochNathalie BleimlingRoger S GoodyMatthias Philipp Müller
Published in: Acta crystallographica. Section F, Structural biology communications (2018)
The structure of the tandem lipid-binding PX and pleckstrin-homology (PH) domains of the Cdc42 GTPase-activating protein Bem3 from Saccharomyces cerevisiae (strain S288c) has been determined to a resolution of 2.2 Å (Rwork = 21.1%, Rfree = 23.4%). It shows that the domains adopt a relative orientation that enables them to simultaneously bind to a membrane and suggests possible cooperativity in membrane binding.
Keyphrases
  • saccharomyces cerevisiae
  • binding protein
  • signaling pathway
  • dna binding
  • cell cycle
  • protein protein
  • amino acid
  • small molecule