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Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae
- 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.
- Subjects :
- 0301 basic medicine
Saccharomyces cerevisiae Proteins
Stereochemistry
Saccharomyces cerevisiae
Biophysics
Cooperativity
CDC42
PX domain
Biochemistry
Protein Structure, Secondary
Research Communications
03 medical and health sciences
Structural Biology
Genetics
Protein Interaction Domains and Motifs
Amino Acid Sequence
phosphatidylinositol phosphates
biology
Tandem
Strain (chemistry)
Bem3
Chemistry
PH domain
GTPase-Activating Proteins
PIP
pleckstrin homology
Condensed Matter Physics
biology.organism_classification
phox
Protein Structure, Tertiary
Pleckstrin homology domain
030104 developmental biology
Membrane
Crystallization
Subjects
Details
- ISSN :
- 2053230X
- Volume :
- 74
- Issue :
- Pt 5
- Database :
- OpenAIRE
- Journal :
- Acta crystallographica. Section F, Structural biology communications
- Accession number :
- edsair.doi.dedup.....fc468d2cf4c746a04aecf2d69daa873d