1VFY: Phosphatidylinositol-3-Phosphate Binding Fyve Domain Of Vps27p Protein From Saccharomyces Cerevisiae

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.
PDB ID: 1VFYDownload
MMDB ID: 10336
PDB Deposition Date: 1999/4/26
Updated in MMDB: 2003/12
Experimental Method:
x-ray diffraction
Resolution: 1.15  Å
Source Organism:
Similar Structures:
Biological Unit for 1VFY: monomeric; determined by author
Molecular Components in 1VFY
Label Count Molecule
Protein (1 molecule)
Phosphatidylinositol-3-phosphate Binding Fyve Domain of Protein Vps27(Gene symbol: VPS27)
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB