| Autor: |
Cedergren-Zeppezauer, Eila S., Goonesekere, Nalin C.W., Rozycki, Michael D., Myslik, James C., Dauter, Zbigniew, Lindberg, Uno, Schutt, Clarence E. |
| Zdroj: |
JMB Online (Journal of Molecular Biology); July 1994, Vol. 240 Issue: 5 p459-475, 17p |
| Abstrakt: |
Profilin regulates the behavior of the eukaryotic microfilament system through its interaction with non-filamentous actin. It also binds several ligands, including poly(l-proline) and the membrane phospholipid phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Bovine profilin crystals (space group C2; a= 69·15 Å, b= 34·59 Å, c= 52·49 Å; α = γ = 90°, β = 92·56°) were grown from a mixture of poly(ethylene glycol) 400 and ammonium sulfate. X-ray diffraction data were collected on an imaging plate scanner at the DORIS storage ring (DESY, Hamburg), and were phased by molecular replacement, using a search model derived from the 2·55 Å structure of profilin complexed to β-actin. The refined model of bovine profilin has a crystallographic R-factor of 16·5% in the resolution range 6·0 to 2·0 Å and includes 128 water molecules, several of which form hydrogen bonds to stabilize unconventional turns. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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