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

Acta Crystallogr F Struct Biol Commun. 2018 May 1;74(Pt 5):315-321. doi: 10.1107/S2053230X18005915. Epub 2018 Apr 24.

Abstract

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.

Keywords: Bem3; PH domain; PIP; PX domain; Saccharomyces cerevisiae; phosphatidylinositol phosphates; phox; pleckstrin homology.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Crystallization / methods
  • GTPase-Activating Proteins / chemistry*
  • GTPase-Activating Proteins / genetics*
  • Protein Interaction Domains and Motifs / genetics*
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / genetics*

Substances

  • BEM3 protein, S cerevisiae
  • GTPase-Activating Proteins
  • Saccharomyces cerevisiae Proteins