The glutamate switch is present in all seven clades of AAA+ protein.

Journal article

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.

Authors: Mogni, M; Costa, A; Ioannou, C; Bell, S

• Publication status: Published
• Journal: Biochemistry
• Volume: 48
• Issue: 37
• Pages: 8774-8775
• Publication date: 2009-09-01
• DOI: 10.1021/bi9012512
• EISSN: 1520-4995
• ISSN: 0006-2960
• Language: English
• Keywords: Threonine; DnaB Helicases; Glutamic Acid; Structural Homology, Protein; Archaeal Proteins; Substrate Specificity; Multigene Family; Sulfolobus solfataricus; Catalytic Domain; Adenosine Triphosphate; MCM1 Protein; Amino Acid Motifs