A large conformational change of the translocation ATPase SecA.
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ABSTRACT:
SUBMITTER: Osborne AR
PROVIDER: S-EPMC491988 | biostudies-literature | 2004 Jul
REPOSITORIES: biostudies-literature
Publications
A large conformational change of the translocation ATPase SecA.
Osborne Andrew R AR Clemons William M WM Rapoport Tom A TA
Proceedings of the National Academy of Sciences of the United States of America 20040715 30
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-A 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 polypeptid ...[more]
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