1vfy

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Image:1vfy.gif

1vfy, resolution 1.15Å

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PHOSPHATIDYLINOSITOL-3-PHOSPHATE BINDING FYVE DOMAIN OF VPS27P PROTEIN FROM SACCHAROMYCES CEREVISIAE

Overview

Phosphatidylinositol 3-phosphate regulates membrane trafficking and, signaling pathways by interacting with the FYVE domains of target, proteins. The 1.15 A structure of the Vps27p FYVE domain reveals two, antiparallel beta sheets and an alpha helix stabilized by two Zn2+-binding, clusters. The core secondary structures are similar to a rabphilin-3A, Zn2+-binding domain and to the C1 and LIM domains. Phosphatidylinositol, 3-phosphate binds to a pocket formed by the (R/K)(R/K)HHCR motif. A, lattice contact shows how anionic ligands can interact with the, phosphatidylinositol 3-phosphate-binding site. The tip of the FYVE domain, has basic and hydrophobic surfaces positioned so that nonspecific, interactions with the phospholipid bilayer can abet specific binding to, phosphatidylinositol 3-phosphate.

About this Structure

1VFY is a Single protein structure of sequence from Saccharomyces cerevisiae with ZN as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p., Misra S, Hurley JH, Cell. 1999 May 28;97(5):657-66. PMID:10367894

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