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Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae
Journal article   Open access  Peer reviewed

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

Imtiaz Ali, Sungmin Eu, Daniel Koch, Nathalie Bleimling, Roger S. Goody and Matthias P. Mueller
Acta crystallographica. Section F, Structural biology communications, Vol.74(5), pp.315-321
05/2018
DOI: https://doi.org/10.1107/S2053230X18005915
PMCID: PMC5931145
PMID: 29718000

Abstract

Biochemical Research Methods Biochemistry & Molecular Biology Biophysics Crystallography Life Sciences & Biomedicine Physical Sciences Science & Technology
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 angstrom (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.
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