Metal-binding sites at the active site of restriction endonuclease BamHI can conform to a one-ion mechanism

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9 Citations (Scopus)

Abstract

The number of metal ions required for phosphoryl transfer in restriction endonucleases is still an unresolved question in molecular biology. The two Ca2+ and Mn2+ ions observed in the pre- and post-reactive complexes of BamHI conform to the classical two-metal ion choreography. We probed the Mg2+ 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.

Original languageEnglish
Pages (from-to)73-78
Number of pages6
JournalBiological Chemistry
Volume388
Issue number1
DOIs
Publication statusPublished - Jan 1 2007

Keywords

  • Metal ion cofactors
  • Phosphoryl transfer
  • Restriction endonucleases
  • Two-metal ion mechanism

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Clinical Biochemistry

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