Structure of the tandem PX‐PH domains of Bem3 from Saccharomyces cerevisiae. Issue 5 (2nd May 2018)

• Record Type: Journal Article
• Authors: Ali, Imtiaz; Eu, Sungmin; Koch, Daniel; Bleimling, Nathalie; Goody, Roger S.; Müller, Matthias P.
• Is Part Of: Acta crystallographica. Volume 74:Issue 5(2018:May)
• Page Start: 315
• Page End: 321
• Publication Date: 2018-05-02
• Subjects: PX domain -- PH domain -- phox -- pleckstrin homology -- phosphatidylinositol phosphates -- PIP -- Saccharomyces cerevisiae -- Bem3; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X18005915
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : The structure of the putative membrane‐binding tandem PX‐PH domain module of the yeast protein Bem3 is reported. 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 ( R work = 21.1%, R free = 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.