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

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 ori...

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Autores principales: Ali, Imtiaz, Eu, Sungmin, Koch, Daniel, Bleimling, Nathalie, Goody, Roger S., Müller, Matthias P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2018
Materias:
Research Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5931145/
https://www.ncbi.nlm.nih.gov/pubmed/29718000
http://dx.doi.org/10.1107/S2053230X18005915
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author Ali, Imtiaz
Eu, Sungmin
Koch, Daniel
Bleimling, Nathalie
Goody, Roger S.
Müller, Matthias P.
author_facet Ali, Imtiaz
Eu, Sungmin
Koch, Daniel
Bleimling, Nathalie
Goody, Roger S.
Müller, Matthias P.
author_sort Ali, Imtiaz
collection PubMed
description 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.
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spelling pubmed-59311452018-05-11 Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae Ali, Imtiaz Eu, Sungmin Koch, Daniel Bleimling, Nathalie Goody, Roger S. Müller, Matthias P. Acta Crystallogr F Struct Biol Commun Research Communications 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. International Union of Crystallography 2018-04-24 /pmc/articles/PMC5931145/ /pubmed/29718000 http://dx.doi.org/10.1107/S2053230X18005915 Text en © Ali et al. 2018 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/2.0/uk/
spellingShingle Research Communications
Ali, Imtiaz
Eu, Sungmin
Koch, Daniel
Bleimling, Nathalie
Goody, Roger S.
Müller, Matthias P.
Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae
title Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae
title_full Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae
title_fullStr Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae
title_full_unstemmed Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae
title_short Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae
title_sort structure of the tandem px-ph domains of bem3 from saccharomyces cerevisiae
topic Research Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5931145/
https://www.ncbi.nlm.nih.gov/pubmed/29718000
http://dx.doi.org/10.1107/S2053230X18005915
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