1DVP

CRYSTAL STRUCTURE OF THE VHS AND FYVE TANDEM DOMAINS OF HRS, A PROTEIN INVOLVED IN MEMBRANE TRAFFICKING AND SIGNAL TRANSDUCTION

Summary for 1DVP

• Entry DOI: 10.2210/pdb1dvp/pdb
• Related: 1VFY
• Descriptor: HEPATOCYTE GROWTH FACTOR-REGULATED TYROSINE KINASE SUBSTRATE, ZINC ION, CITRIC ACID, ... (4 entities in total)
• Functional Keywords: hrs, vhs, fyve, zinc finger, superhelix, transferase
• Biological source: Drosophila melanogaster (fruit fly)
• Total number of polymer chains: 1
• Total formula weight: 25438.81

Authors

Mao, Y.,Nickitenko, A.,Duan, X.,Lloyd, T.E.,Wu, M.N.,Bellen, H.,Quiocho, F.A. (deposition date: 2000-01-21, release date: 2000-03-06, Last modification date: 2024-02-07)

Primary citation

Mao, Y.,Nickitenko, A.,Duan, X.,Lloyd, T.E.,Wu, M.N.,Bellen, H.,Quiocho, F.A.
Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction.
Cell(Cambridge,Mass.), 100:447-456, 2000

PubMed Abstract: We have determined the 2 A 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 alpha 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.

PubMed: 10693761
DOI: 10.1016/S0092-8674(00)80680-7

Experimental method

X-RAY DIFFRACTION (2 Å)