3DIN
Crystal structure of the protein-translocation complex formed by the SecY channel and the SecA ATPase
Summary for 3DIN
| Entry DOI | 10.2210/pdb3din/pdb |
| Descriptor | Protein translocase subunit secA, Preprotein translocase subunit SecY, Preprotein translocase subunit secE, ... (7 entities in total) |
| Functional Keywords | protein translocation, membrane protein, atpase, atp-binding, inner membrane, nucleotide-binding, protein transport, transport, transmembrane |
| Biological source | Thermotoga maritima MSB8 More |
| Cellular location | Cell inner membrane ; Peripheral membrane protein ; Cytoplasmic side : Q9X1R4 Cell inner membrane; Multi-pass membrane protein: Q9X1I9 Cell inner membrane; Single-pass membrane protein: P35874 |
| Total number of polymer chains | 8 |
| Total formula weight | 329908.03 |
| Authors | Zimmer, J.,Nam, Y.,Rapoport, T.A. (deposition date: 2008-06-20, release date: 2008-10-07, Last modification date: 2023-08-30) |
| Primary citation | Zimmer, J.,Nam, Y.,Rapoport, T.A. Structure of a complex of the ATPase SecA and the protein-translocation channel. Nature, 455:936-943, 2008 Cited by PubMed Abstract: Most proteins are secreted from bacteria by the interaction of the cytoplasmic SecA ATPase with a membrane channel, formed by the heterotrimeric SecY complex. Here we report the crystal structure of SecA bound to the SecY complex, with a maximum resolution of 4.5 ångström (A), obtained for components from Thermotoga maritima. One copy of SecA in an intermediate state of ATP hydrolysis is bound to one molecule of the SecY complex. Both partners undergo important conformational changes on interaction. The polypeptide-cross-linking domain of SecA makes a large conformational change that could capture the translocation substrate in a 'clamp'. Polypeptide movement through the SecY channel could be achieved by the motion of a 'two-helix finger' of SecA inside the cytoplasmic funnel of SecY, and by the coordinated tightening and widening of SecA's clamp above the SecY pore. SecA binding generates a 'window' at the lateral gate of the SecY channel and it displaces the plug domain, preparing the channel for signal sequence binding and channel opening. PubMed: 18923516DOI: 10.1038/nature07335 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.5 Å) |
Structure validation
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