5loz
From Proteopedia
STRUCTURE OF YEAST ENT1 ENTH DOMAIN
Structural highlights
Function[ENT1_YEAST] Binds to membranes enriched in phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Required for endocytosis and localization of actin. Negatively regulated via phosphorylation.[1] [2] [3] Publication Abstract from PubMedMembers of the Epsin protein family regulate the ubiquitin/clathrin-dependent trafficking of transmembrane proteins. The yeast Epsin-1 (ent1) gene was cloned and expressed in Escherichia coli. The protein product of a construct containing the ENTH-UIM modules was purified to homogeneity and subjected to crystallization screening using the sitting-drop vapour-diffusion method. Refined conditions containing polyethylene glycol 3350 and Tacsimate yielded thin rod-like crystals. X-ray analysis revealed that the crystallographic symmetry is primitive orthorhombic, space group P222, with unit-cell parameters a = 32.7, b = 35.5, c = 110.6 A and a diffraction limit of 2.3 A. Matthews coefficient calculations suggested that the crystal contained only the ENTH domain. This was corroborated by Coomassie Blue-stained SDS-PAGE analysis of dissolved crystals. Purification and crystallization of yeast Ent1 ENTH domain.,Tanner N, Prag G Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jul 1;68(Pt 7):820-3. doi:, 10.1107/S1744309112022488. Epub 2012 Jun 28. PMID:22750874[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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