1tf2
From Proteopedia
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Crystal structure of SecA:ADP in an open conformation from Bacillus Subtilis
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
Page seeded by OCA on Wed Nov 21 03:12:43 2007
Categories: Bacillus subtilis | Single protein | Jr., W.M.Clemons. | Osborne, A.R. | Rapoport, T.A. | ADP | MG | Atpase | Helicase | Secretion | Translocation
