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1vfy
From Proteopedia
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|PDB= 1vfy |SIZE=350|CAPTION= <scene name='initialview01'>1vfy</scene>, resolution 1.15Å | |PDB= 1vfy |SIZE=350|CAPTION= <scene name='initialview01'>1vfy</scene>, resolution 1.15Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= VPS27 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= VPS27 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vfy OCA], [http://www.ebi.ac.uk/pdbsum/1vfy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vfy RCSB]</span> | ||
}} | }} | ||
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[[Category: Hurley, J H.]] | [[Category: Hurley, J H.]] | ||
[[Category: Misra, S.]] | [[Category: Misra, S.]] | ||
| - | [[Category: ZN]] | ||
[[Category: endosome maturation]] | [[Category: endosome maturation]] | ||
[[Category: fyve domain]] | [[Category: fyve domain]] | ||
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[[Category: transport protein]] | [[Category: transport protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:23:51 2008'' |
Revision as of 21:23, 30 March 2008
| |||||||
| , resolution 1.15Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | VPS27 (Saccharomyces cerevisiae) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PHOSPHATIDYLINOSITOL-3-PHOSPHATE BINDING FYVE DOMAIN OF VPS27P PROTEIN FROM SACCHAROMYCES CEREVISIAE
Overview
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.
About this Structure
1VFY is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p., Misra S, Hurley JH, Cell. 1999 May 28;97(5):657-66. PMID:10367894
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