A large conformational change of the translocation ATPase SecA.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 15256599.
- Also identified by PMC identifier 491988.
- No licence information is recorded for this record.
- Because redistribution is not established, this page shows the abstract only. Follow the links below for the full text.
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-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 polypeptides. We propose that the open form of SecA represents an activated state.
Medical subject headings
- Adenosine Triphosphatases
- Bacterial Proteins
- Membrane Transport Proteins