TY  - JOUR
AU  - Elfrink, K.
AU  - Nagel-Steger, L.
AU  - Riesner, D.
TI  - Interaction of the cellular prion protein with raft-like lipid membranes
JO  - Biological chemistry
VL  - 388
SN  - 1431-6730
CY  - Berlin [u.a.]
PB  - de Gruyter
M1  - PreJuSER-60183
SP  - 79 - 89
PY  - 2007
N1  - Record converted from VDB: 12.11.2012
AB  - 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.
KW  - Binding Sites
KW  - Calcium: metabolism
KW  - Crystallography, X-Ray
KW  - Deoxyribonuclease BamHI: chemistry
KW  - Deoxyribonuclease BamHI: metabolism
KW  - Magnesium: metabolism
KW  - Manganese: metabolism
KW  - Metals: metabolism
KW  - Models, Molecular
KW  - Protein Structure, Secondary
KW  - Structure-Activity Relationship
KW  - Metals (NLM Chemicals)
KW  - Magnesium (NLM Chemicals)
KW  - Manganese (NLM Chemicals)
KW  - Calcium (NLM Chemicals)
KW  - Deoxyribonuclease BamHI (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:17214552
UR  - <Go to ISI:>//WOS:000243366400010
UR  - https://juser.fz-juelich.de/record/60183
ER  -