Publication: A large conformational change of the translocation ATPase SecA
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Date
2004
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National Academy of Sciences
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Osborne, A. R., W. M. Clemons, and T. A. Rapoport. 2004. “A Large Conformational Change of the Translocation ATPase SecA.” Proceedings of the National Academy of Sciences 101 (30): 10937–42. doi:10.1073/pnas.0401742101.
Abstract
The ATPase SecA mediates the posttranslational translocation of a wide range of polypeptide substrates through the SecY channel in the cytoplasmic membrane of bacteria. We have determined the crystal structure of a monomeric form of Bacillus subtilis SecA at a 2.2-Angstrom resolution. A comparison with the previously determined structures of SecA reveals a nucleotide-independent, large conformational change that opens a deep groove similar to that in other proteins that interact with diverse polypeptides. We propose that the open form of SecA represents an activated state.
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