PDB ID or protein name

1vfy » FYVE domain of Vps27 protein

1vfy » FYVE domain of Vps27 protein
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Topology in Vacuole membrane
Topologylumenal side
cytoplasmic side
1vfy » FYVE domain of Vps27 protein
Depth 3.7 ± 1.8 Å
Tilt Angle 24 ± 19°
ΔGtransfer -4.2 kcal/mol
Links to 1vfy PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology cytoplasmic
Resolution 1.15 Å
Other PDB entries representing this structure none
Number of subunits 1
Experimental Verification for 1vfy » FYVE domain of Vps27 protein
This FYVE domain strongly associates with lipid bilayers in the presence of PtdIns(3)P lipids (Blatner et al. 2004). L185 and L186 penetrate the hydrophobic slab according to our results. This is consistent with binding and mutagenesis studies: mutations of L185 and L186 reduced the monolayer penetration, while mutations of K181 and K182 had only a slight effect (Stahelin et al. 2002). Membrane binding affinity of an isolated FYVE domain is -10.5 kcal/mol (Blatner et al. 2004), which is higher than the calculated transfer energy due to specific binding of PtdIns(3)P.
3 references
Blatner NR, Stahelin RV, Diraviyam K, Hawkins PT, Hong W, Murray D, Cho W. 2004. The molecular basis of the differential subcellular localization of FYVE domains. J Biol Chem. 279:53818-27. PubMed
Diraviyam K, Stahelin RV, Cho W, Murray D. 2003. Computer modeling of the membrane interaction of FYVE domains. J Mol Biol. 328:721-36. PubMed
Stahelin RV, Long F, Diraviyam K, Bruzik KS, Murray D, Cho W. 2002. Phosphatidylinositol 3-phosphate induces the membrane penetration of the FYVE domains of Vps27p and Hrs. J Biol Chem. 277: 26379-26388. PubMed
Comments on 1vfy » FYVE domain of Vps27 protein
This orientation is in agreement with results of computational modeling of FYVE domains based on the electrostatic interactions (Diraviyam et al. 2003). However, FYVE domain penetrates by ~10A deeper into the membrane according to our results: nonpolar residues are inserted in the membrane hydrocarbon core, not in the head group region.