1VFY

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

Summary for 1VFY

• Entry DOI: 10.2210/pdb1vfy/pdb
• Descriptor: PHOSPHATIDYLINOSITOL-3-PHOSPHATE BINDING FYVE DOMAIN OF PROTEIN VPS27, ZINC ION (3 entities in total)
• Functional Keywords: fyve domain, endosome maturation, intracellular trafficking, transport protein
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Endosome membrane; Peripheral membrane protein; Cytoplasmic side: P40343
• Total number of polymer chains: 1
• Total formula weight: 8402.13

Authors

Hurley, J.H.,Misra, S. (deposition date: 1999-04-26, release date: 1999-05-06, Last modification date: 2023-12-27)

Primary citation

Misra, S.,Hurley, J.H.
Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p.
Cell(Cambridge,Mass.), 97:657-666, 1999

PubMed Abstract: 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.

PubMed: 10367894
DOI: 10.1016/S0092-8674(00)80776-X

Experimental method

X-RAY DIFFRACTION (1.15 Å)