Structural highlights
Function
BEM3_YEAST GTPase-activating protein (GAP) for CDC42 and less efficiently for RHO1. Negative regulator of the pheromone-response pathway through the STE20 protein kinase.[1] [2]
Publication Abstract from PubMed
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 A (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.
Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae.,Ali I, Eu S, Koch D, Bleimling N, Goody RS, Muller MP Acta Crystallogr F Struct Biol Commun. 2018 May 1;74(Pt 5):315-321. doi:, 10.1107/S2053230X18005915. Epub 2018 Apr 24. PMID:29718000[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zheng Y, Hart MJ, Shinjo K, Evans T, Bender A, Cerione RA. Biochemical comparisons of the Saccharomyces cerevisiae Bem2 and Bem3 proteins. Delineation of a limit Cdc42 GTPase-activating protein domain. J Biol Chem. 1993 Nov 25;268(33):24629-34. PMID:8227021
- ↑ Zheng Y, Cerione R, Bender A. Control of the yeast bud-site assembly GTPase Cdc42. Catalysis of guanine nucleotide exchange by Cdc24 and stimulation of GTPase activity by Bem3. J Biol Chem. 1994 Jan 28;269(4):2369-72. PMID:8300560
- ↑ Ali I, Eu S, Koch D, Bleimling N, Goody RS, Muller MP. Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae. Acta Crystallogr F Struct Biol Commun. 2018 May 1;74(Pt 5):315-321. doi:, 10.1107/S2053230X18005915. Epub 2018 Apr 24. PMID:29718000 doi:http://dx.doi.org/10.1107/S2053230X18005915
