| 1vfy >> FYVE domain of Vps27 protein |
|---|
| Hydrophobic Thickness or Depth | 3.7 Å |
| Tilt Angle | 24° |
| ΔGtransfer | -4.2 kcal/mol |
| Links to 1vfy | PDB Sum, PDB, MSD, MMDB |
| Topology | cytoplasmic side |
| Resolution | 1.15 |
| Primary PDB represention | 1vfy |
| Other PDB entries representing this structure | none |
| Number of TM secondary structures | 0 |
| Membranome | |
| Uniprot | VPS27_YEAST |
  | lumenal side |
| cytoplasmic side |
Comments: 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.
| Verification: 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. |
| References: 3 |
|---|
| 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 |
| 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 |
| 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 |
