%0 Journal Article
%A Elfrink, K.
%A Nagel-Steger, L.
%A Riesner, D.
%T Interaction of the cellular prion protein with raft-like lipid membranes
%J Biological chemistry
%V 388
%@ 1431-6730
%C Berlin [u.a.]
%I de Gruyter
%M PreJuSER-60183
%P 79 - 89
%D 2007
%Z Record converted from VDB: 12.11.2012
%X 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.
%K Binding Sites
%K Calcium: metabolism
%K Crystallography, X-Ray
%K Deoxyribonuclease BamHI: chemistry
%K Deoxyribonuclease BamHI: metabolism
%K Magnesium: metabolism
%K Manganese: metabolism
%K Metals: metabolism
%K Models, Molecular
%K Protein Structure, Secondary
%K Structure-Activity Relationship
%K Metals (NLM Chemicals)
%K Magnesium (NLM Chemicals)
%K Manganese (NLM Chemicals)
%K Calcium (NLM Chemicals)
%K Deoxyribonuclease BamHI (NLM Chemicals)
%K J (WoSType)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:17214552
%U <Go to ISI:>//WOS:000243366400010
%U https://juser.fz-juelich.de/record/60183