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@ARTICLE{Elfrink:60183,
author = {Elfrink, K. and Nagel-Steger, L. and Riesner, D.},
title = {{I}nteraction of the cellular prion protein with raft-like
lipid membranes},
journal = {Biological chemistry},
volume = {388},
issn = {1431-6730},
address = {Berlin [u.a.]},
publisher = {de Gruyter},
reportid = {PreJuSER-60183},
pages = {79 - 89},
year = {2007},
note = {Record converted from VDB: 12.11.2012},
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.},
keywords = {Binding Sites / Calcium: metabolism / Crystallography,
X-Ray / Deoxyribonuclease BamHI: chemistry /
Deoxyribonuclease BamHI: metabolism / Magnesium: metabolism
/ Manganese: metabolism / Metals: metabolism / Models,
Molecular / Protein Structure, Secondary /
Structure-Activity Relationship / Metals (NLM Chemicals) /
Magnesium (NLM Chemicals) / Manganese (NLM Chemicals) /
Calcium (NLM Chemicals) / Deoxyribonuclease BamHI (NLM
Chemicals) / J (WoSType)},
cin = {INB-2},
ddc = {540},
cid = {I:(DE-Juel1)VDB805},
pnm = {Funktion und Dysfunktion des Nervensystems},
pid = {G:(DE-Juel1)FUEK409},
shelfmark = {Biochemistry $\&$ Molecular Biology},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:17214552},
UT = {WOS:000243366400010},
url = {https://juser.fz-juelich.de/record/60183},
}