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2. Nucleotide exchange from the high-affinity ATP-binding site in SecA is the rate-limiting step in the ATPase cycle of the soluble enzyme and occurs through a specialized conformational state. Fak JJ, Itkin A, Ciobanu DD, Lin EC, Song XJ, Chou YT, Gierasch LM, Hunt JF. Biochemistry; 2004 Jun 15; 43(23):7307-27. PubMed ID: 15182175 [Abstract] [Full Text] [Related]
5. Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase. Duong F. EMBO J; 2003 Sep 01; 22(17):4375-84. PubMed ID: 12941690 [Abstract] [Full Text] [Related]
6. Bacillus subtilis SecA ATPase exists as an antiparallel dimer in solution. Ding H, Hunt JF, Mukerji I, Oliver D. Biochemistry; 2003 Jul 29; 42(29):8729-38. PubMed ID: 12873133 [Abstract] [Full Text] [Related]
15. Mechanism of conformational coupling in SecA: Key role of hydrogen-bonding networks and water interactions. Milenkovic S, Bondar AN. Biochim Biophys Acta; 2016 Feb 29; 1858(2):374-85. PubMed ID: 26607006 [Abstract] [Full Text] [Related]
19. Electron microscopic visualization of asymmetric precursor translocation intermediates: SecA functions as a dimer. Tang Y, Pan X, Tai PC, Sui S. Sci China Life Sci; 2010 Sep 29; 53(9):1049-56. PubMed ID: 21104364 [Abstract] [Full Text] [Related]