2VDA
Solution structure of the SecA-signal peptide complex
Summary for 2VDA
| Entry DOI | 10.2210/pdb2vda/pdb |
| Related | 1M6N 1TF5 1TM6 2FSF |
| Descriptor | TRANSLOCASE SUBUNIT SECA, MALTOPORIN (2 entities in total) |
| Functional Keywords | sugar transport, protein transport, protein targeting, transmembrane, outer membrane, signal peptide, paramagnetic relaxation enhancement, translocase, ion transport, translocation, protein secretion, nucleotide-binding, seca, porin, membrane, transport, atp-binding, high molecular weight complex |
| Biological source | ESCHERICHIA COLI More |
| Cellular location | Cell inner membrane; Peripheral membrane protein; Cytoplasmic side: P10408 Cell outer membrane ; Multi-pass membrane protein : Q8CVI4 |
| Total number of polymer chains | 2 |
| Total formula weight | 96990.49 |
| Authors | Gelis, I.,Bonvin, A.M.J.J.,Keramisanou, D.,Koukaki, M.,Gouridis, G.,Karamanou, S.,Economou, A.,Kalodimos, C.G. (deposition date: 2007-10-01, release date: 2007-11-27, Last modification date: 2024-05-15) |
| Primary citation | Gelis, I.,Bonvin, A.M.J.J.,Keramisanou, D.,Koukaki, M.,Gouridis, G.,Karamanou, S.,Economou, A.,Kalodimos, C.G. Structural Basis for Signal-Sequence Recognition by the Translocase Motor Seca as Determined by NMR Cell(Cambridge,Mass.), 131:756-, 2007 Cited by PubMed Abstract: Recognition of signal sequences by cognate receptors controls the entry of virtually all proteins to export pathways. Despite its importance, this process remains poorly understood. Here, we present the solution structure of a signal peptide bound to SecA, the 204 kDa ATPase motor of the Sec translocase. Upon encounter, the signal peptide forms an alpha-helix that inserts into a flexible and elongated groove in SecA. The mode of binding is bimodal, with both hydrophobic and electrostatic interactions mediating recognition. The same groove is used by SecA to recognize a diverse set of signal sequences. Impairment of the signal-peptide binding to SecA results in significant translocation defects. The C-terminal tail of SecA occludes the groove and inhibits signal-peptide binding, but autoinhibition is relieved by the SecB chaperone. Finally, it is shown that SecA interconverts between two conformations in solution, suggesting a simple mechanism for polypeptide translocation. PubMed: 18022369DOI: 10.1016/J.CELL.2007.09.039 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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