Abstract
Recent work has identified a "glutamate switch" in six of the seven clades of AAA+ ATPases. The glutamate switch acts to transduce information regarding substrate binding to the ATPase active site. We provide biochemical evidence that a highly conserved threonine residue acts as a glutamate switch in the replicative helicase, MCM, and, thus, reveal that the glutamate switch is a feature common to all seven AAA+ clades.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphate / chemistry
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Adenosine Triphosphate / metabolism
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Amino Acid Motifs
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Archaeal Proteins / chemistry*
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Archaeal Proteins / genetics
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Archaeal Proteins / metabolism
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Catalytic Domain / genetics
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DnaB Helicases / chemistry*
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DnaB Helicases / genetics
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DnaB Helicases / metabolism
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Glutamic Acid / chemistry*
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Glutamic Acid / metabolism*
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Minichromosome Maintenance 1 Protein / chemistry*
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Minichromosome Maintenance 1 Protein / genetics
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Minichromosome Maintenance 1 Protein / metabolism
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Multigene Family
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Structural Homology, Protein*
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Substrate Specificity / genetics
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Sulfolobus solfataricus / enzymology
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Threonine / chemistry
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Threonine / genetics
Substances
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Archaeal Proteins
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Minichromosome Maintenance 1 Protein
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Threonine
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Glutamic Acid
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Adenosine Triphosphate
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DnaB Helicases