2vda
From Proteopedia
Solution structure of the SecA-signal peptide complex
Structural highlights
Function[SECA_ECOLI] Required for protein export, interacts with the SecYEG preprotein conducting channel. SecA has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.[1] [LAMB_ECOL6] Involved in the transport of maltose and maltodextrins (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedRecognition 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. Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR.,Gelis I, Bonvin AM, Keramisanou D, Koukaki M, Gouridis G, Karamanou S, Economou A, Kalodimos CG Cell. 2007 Nov 16;131(4):756-69. PMID:18022369[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. Loading citation details.. Citations 59 reviews cite this structure No citations found See AlsoReferences
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Categories: Bacillus coli migula 1895 | Large Structures | Bonvin, A M.J J | Economou, A | Gelis, I | Gouridis, G | Kalodimos, C G | Karamanou, S | Keramisanou, D | Koukaki, M | Atp-binding | High molecular weight complex | Ion transport | Membrane | Nucleotide-binding | Outer membrane | Paramagnetic relaxation enhancement | Porin | Protein secretion | Protein targeting | Protein transport | Seca | Signal peptide | Sugar transport | Translocase | Translocation | Transmembrane | Transport
