Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction

Yuxin Mao, Alexei Nickitenko, Xiaoqun Duan, Thomas E. Lloyd, Mark N. Wu, Hugo Bellen, Florante A. Quiocho

Research output: Contribution to journalArticle

Abstract

We have determined the 2 Å X-ray structure of the 219-residue N-terminal VHS and FYVE tandem domain unit of Drosophila Hrs. The unit assumes a pyramidal structure in which the much larger VHS domain (residues 1-153) forms a rectangular base and the FYVE domain occupies the apical end. The VHS domain is comprised of an unusual 'superhelix' of eight α helices, and the FYVE domain is mainly built of loops, two double-stranded antiparallel sheets, and a helix stabilized by two tetrahedrally coordinated zinc atoms. The two-domain structure forms an exact 2-fold-related homodimer through antiparallel association of mainly FYVE domains. Dimerization creates two identical pockets designed for binding ligands with multiple negative charges such as citrate or phosphatidylinositol 3-phosphate.

Original languageEnglish (US)
Pages (from-to)447-456
Number of pages10
JournalCell
Volume100
Issue number4
DOIs
StatePublished - Feb 18 2000
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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