4N5A
Crystal structure of Efr3
Summary for 4N5A
| Entry DOI | 10.2210/pdb4n5a/pdb |
| Related | 4N5C |
| Descriptor | Protein EFR3 (1 entity in total) |
| Functional Keywords | heat-like repeats, component of stt4 complex, ypp1, plasma membrane, protein binding |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 64781.94 |
| Authors | Wu, X.,Chi, R.J.,Baskin, J.M.,Lucast, L.,Burd, C.G.,De Camilli, P.,Reinisch, K.M. (deposition date: 2013-10-09, release date: 2014-01-22, Last modification date: 2024-10-30) |
| Primary citation | Wu, X.,Chi, R.J.,Baskin, J.M.,Lucast, L.,Burd, C.G.,De Camilli, P.,Reinisch, K.M. Structural insights into assembly and regulation of the plasma membrane phosphatidylinositol 4-kinase complex. Dev.Cell, 28:19-29, 2014 Cited by PubMed Abstract: Plasma membrane PI4P helps determine the identity of this membrane and plays a key role in signal transduction as the precursor of PI(4,5)P2 and its metabolites. Here, we report the atomic structure of the protein scaffold that is required for the plasma membrane localization and function of Stt4/PI4KIIIα, the PI 4-kinase responsible for this PI4P pool. Both proteins of the scaffold, Efr3 and YPP1/TTC7, are composed of α-helical repeats, which are arranged into a rod in Efr3 and a superhelix in Ypp1. A conserved basic patch in Efr3, which binds acidic phospholipids, anchors the complex to the plasma membrane. Stt4/PI4KIIIα is recruited by interacting with the Ypp1 C-terminal lobe, which also binds to unstructured regions in the Efr3 C terminus. Phosphorylation of this Efr3 region counteracts Ypp1 binding, thus providing a mechanism through which Stt4/PI4KIIIα recruitment, and thus a metabolic reaction of fundamental importance in cell physiology, can be regulated. PubMed: 24360784DOI: 10.1016/j.devcel.2013.11.012 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.204 Å) |
Structure validation
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