Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae.
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ABSTRACT:
SUBMITTER: Ali I
PROVIDER: S-EPMC5931145 | biostudies-literature | 2018 May
REPOSITORIES: biostudies-literature
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Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae.
Ali Imtiaz I Eu Sungmin S Koch Daniel D Bleimling Nathalie N Goody Roger S RS Müller Matthias P MP
Acta crystallographica. Section F, Structural biology communications 20180424 Pt 5
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<sub>work</sub> = 21.1%, R<sub>free</sub> = 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. ...[more]
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