7XHA
Structure of the SecA/SecYE/proOmpA(4Y)-sfGFP complex with ADP.BeF3-.
Summary for 7XHA
| Entry DOI | 10.2210/pdb7xha/pdb |
| EMDB information | 33192 |
| Descriptor | Protein translocase subunit SecA, Protein translocase subunit SecY, Protein translocase subunit SecE, ... (7 entities in total) |
| Functional Keywords | seca atpase, membrane protein, translocate, translocase |
| Biological source | Bacillus subtilis subsp. subtilis str. 168 More |
| Total number of polymer chains | 4 |
| Total formula weight | 177031.07 |
| Authors | |
| Primary citation | Dong, L.,Yang, S.,Chen, J.,Wu, X.,Sun, D.,Song, C.,Li, L. Structural basis of SecA-mediated protein translocation. Proc.Natl.Acad.Sci.USA, 120:e2208070120-e2208070120, 2023 Cited by PubMed Abstract: Secretory proteins are cotranslationally or posttranslationally translocated across lipid membranes via a protein-conducting channel named SecY in prokaryotes and Sec61 in eukaryotes. The vast majority of secretory proteins in bacteria are driven through the channel posttranslationally by SecA, a highly conserved ATPase. How a polypeptide chain is moved by SecA through the SecY channel is poorly understood. Here, we report electron cryomicroscopy structures of the active SecA-SecY translocon with a polypeptide substrate. The substrate is captured in different translocation states when clamped by SecA with different nucleotides. Upon binding of an ATP analog, SecA undergoes global conformational changes to push the polypeptide substrate toward the channel in a way similar to how the RecA-like helicases translocate their nucleic acid substrates. The movements of the polypeptide substrates in the SecA-SecY translocon share a similar structural basis to those in the ribosome-SecY complex during cotranslational translocation. PubMed: 36598944DOI: 10.1073/pnas.2208070120 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.35 Å) |
Structure validation
Download full validation report
