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Structure of the tandem PX‐PH domains of Bem3 from Saccharomyces cerevisiae
Author(s) -
Ali Imtiaz,
Eu Sungmin,
Koch Daniel,
Bleimling Nathalie,
Goody Roger S.,
Müller Matthias P.
Publication year - 2018
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x18005915
Subject(s) - saccharomyces cerevisiae , pleckstrin homology domain , cooperativity , tandem , cdc42 , chemistry , gtpase , biophysics , homology (biology) , homology modeling , biochemistry , membrane , biology , amino acid , yeast , materials science , enzyme , composite material
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.