Abstract
Abstract The FYVE domain is a 65‐residue module that contains two tetrahedral zinc coordination centers. The zinc ions are bound by eight cysteine residues in a cross‐braced topology, providing structural stability. The FYVE domain is usually present as a single module or, more rarely, as a tandem repeat in eukaryotic proteins involved in a variety of biological processes including membrane trafficking and phosphoinositide metabolism. The biochemical function of the FYVE domain is the specific recognition of phosphatidylinositol 3‐phosphate [PtdIns(3)P], a phospholipid that is most concentrated in endocytic membranes. Structures, zinc coordination, and PtdIns(3)P binding modes of three FYVE domains have recently been characterized, providing mechanistic insights into their contributions to endocytosis, signal transduction, and cytoskeletal organization.
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