Published in
International Union of Crystallography, Acta Crystallographica Section F: Structural Biology Communications, 5(74), p. 315-321, 2018
DOI: 10.1107/s2053230x18005915
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Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae
,
Nathalie Bleimling,
Roger S. Goody ,
Matthias P. Müller
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Abstract
The structure of the tandem lipid-binding PX and pleckstrin-homology (PH) domains of the Cdc42 GTPase-activating protein Bem3 fromSaccharomyces 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.