1tf2 | pdb_00001tf2
Crystal structure of SecA:ADP in an open conformation from Bacillus Subtilis
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Overview
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.
About this Structure
1TF2 is a Single protein structure of sequence from Bacillus subtilis with MG and ADP as ligands. Full crystallographic information is available from OCA.
Reference
A large conformational change of the translocation ATPase SecA., Osborne AR, Clemons WM Jr, Rapoport TA, Proc Natl Acad Sci U S A. 2004 Jul 27;101(30):10937-42. Epub 2004 Jul 15. PMID:15256599
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