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

Authors :
Sungmin Eu
Nathalie Bleimling
Roger S. Goody
Daniel Koch
Matthias P. Müller
Imtiaz Ali
Source :
Acta Crystallographica. Section F, Structural Biology Communications
Publication Year :
2018

Abstract

The structure of the putative membrane-binding tandem PX-PH domain module of the yeast protein Bem3 is reported.<br />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.

Details

ISSN :
2053230X
Volume :
74
Issue :
Pt 5
Database :
OpenAIRE
Journal :
Acta crystallographica. Section F, Structural biology communications
Accession number :
edsair.doi.dedup.....fc468d2cf4c746a04aecf2d69daa873d