1TF5

Crystal structure of SecA in an open conformation from Bacillus Subtilis

Summary for 1TF5

Entry DOI	10.2210/pdb1tf5/pdb
Related	1TF2
Descriptor	Preprotein translocase secA subunit (2 entities in total)
Functional Keywords	atpase, helicase, translocation, secretion, protein transport
Biological source	Bacillus subtilis
Cellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P28366
Total number of polymer chains	1
Total formula weight	95956.09
Authors	Osborne, A.R.,Clemons Jr., W.M.,Rapoport, T.A. (deposition date: 2004-05-26, release date: 2004-08-03, Last modification date: 2023-08-23)
Primary citation	Osborne, A.R.,Clemons Jr., W.M.,Rapoport, T.A. A large conformational change of the translocation ATPase SecA. Proc.Natl.Acad.Sci.USA, 101:10937-10942, 2004 Cited by PubMed 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. PubMed: 15256599 DOI: 10.1073/pnas.0401742101 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.18 Å)

Structure validation