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Importance of the +73/294 interaction in Escherichia coli RNase P RNA substrate complexes for cleavage and metal ion coordination.
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology.
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology.
2003 (English)In: J Mol Biol, ISSN 0022-2836, Vol. 325, no 4, 697-709 p.Article in journal (Refereed) Published
Place, publisher, year, edition, pages
2003. Vol. 325, no 4, 697-709 p.
Keyword [en]
Base Sequence, Catalytic Domain, Cations; Divalent/metabolism, Endoribonucleases/*metabolism, Escherichia coli/enzymology/genetics/*metabolism, Escherichia coli Proteins, Kinetics, Magnesium/metabolism, Manganese/metabolism, Molecular Sequence Data, Mutation, Nucleic Acid Conformation, RNA; Bacterial/*chemistry/genetics/*metabolism, RNA; Catalytic/*metabolism, Research Support; Non-U.S. Gov't, Ribonuclease P, Substrate Specificity
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URN: urn:nbn:se:uu:diva-73355PubMedID: 12507473OAI: oai:DiVA.org:uu-73355DiVA: diva2:101265
Available from: 2005-06-02 Created: 2005-06-02 Last updated: 2011-01-13

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Brännvall, MathiasKirsebom, Leif

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