6FSF

Crystal structure of the tandem PX-PH-domains of Bem3 from Saccharomyces cerevisiae

Summary for 6FSF

Entry DOI	10.2210/pdb6fsf/pdb
Descriptor	GTPase-activating protein BEM3 (2 entities in total)
Functional Keywords	bem3, px domain, ph domain, phox, pleckstrin homology, phosphatidylinositol phosphates, pip, endocytosis
Biological source	Saccharomyces cerevisiae S288C
Cellular location	Cytoplasm: P32873
Total number of polymer chains	1
Total formula weight	30739.94
Authors	Ali, I.,Eu, S.,Koch, D.,Bleimling, N.,Goody, R.S.,Mueller, M.P. (deposition date: 2018-02-19, release date: 2018-05-02, Last modification date: 2024-05-08)
Primary citation	Ali, I.,Eu, S.,Koch, D.,Bleimling, N.,Goody, R.S.,Muller, M.P. Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae. Acta Crystallogr F Struct Biol Commun, 74:315-321, 2018 Cited by PubMed Abstract: 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 = 21.1%, R = 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. PubMed: 29718000 DOI: 10.1107/S2053230X18005915 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.2 Å)

Structure validation