Interaction of the cellular prion protein with raft-like lipid membranes

Elfrink, K.; Nagel-Steger, L.; Riesner, D.

Journal Article

PreJuSER-60183

Interaction of the cellular prion protein with raft-like lipid membranes

Elfrink, K.FZJ* ; Nagel-Steger, L.FZJ* ; Riesner, D.

2007
de Gruyter Berlin [u.a.]

Biological chemistry 388, 79 - 89 (2007)

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Please use a persistent id in citations: http://hdl.handle.net/2128/18378

Abstract: The number of metal ions required for phosphoryl transfer in restriction endonucleases is still an unresolved question in molecular biology. The two Ca(2+) and Mn(2+) ions observed in the pre- and post-reactive complexes of BamHI conform to the classical two-metal ion choreography. We probed the Mg(2+) cofactor positions at the active site of BamHI by molecular dynamics simulations with one and two metal ions present and identified several catalytically relevant sites. These can mark the pathway of a single ion during catalysis, suggesting its critical role, while a regulatory function is proposed for a possible second ion.

Keyword(s): Binding Sites (MeSH) ; Calcium: metabolism (MeSH) ; Crystallography, X-Ray (MeSH) ; Deoxyribonuclease BamHI: chemistry (MeSH) ; Deoxyribonuclease BamHI: metabolism (MeSH) ; Magnesium: metabolism (MeSH) ; Manganese: metabolism (MeSH) ; Metals: metabolism (MeSH) ; Models, Molecular (MeSH) ; Protein Structure, Secondary (MeSH) ; Structure-Activity Relationship (MeSH) ; Metals ; Magnesium ; Manganese ; Calcium ; Deoxyribonuclease BamHI ; J ; biacore (auto) ; GPI anchor (auto) ; prion (auto) ; PrPc (auto) ; surface plasmon resonance (auto)