4N5C

Crystal structure of Ypp1

Summary for 4N5C

• Entry DOI: 10.2210/pdb4n5c/pdb
• Related: 4N5A
• Descriptor: Cargo-transport protein YPP1 (1 entity in total)
• Functional Keywords: heat-like repeat, component of stt4 complex, efr3, stt4, plasma membrane, protein binding
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Cytoplasmic granule: P46951
• Total number of polymer chains: 8
• Total formula weight: 755514.82

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: 2024-10-16)

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

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: 24360784
DOI: 10.1016/j.devcel.2013.11.012

Experimental method

X-RAY DIFFRACTION (3.25 Å)