3FFV
Crystal Structure Analysis of Syd
Summary for 3FFV
| Entry DOI | 10.2210/pdb3ffv/pdb |
| Descriptor | Protein syd (2 entities in total) |
| Functional Keywords | membrane, translocon, secyeg, syd, nanodisc, cell inner membrane, cell membrane, protein binding |
| Biological source | Escherichia coli |
| Cellular location | Cell inner membrane; Peripheral membrane protein; Cytoplasmic side: P0A8U0 |
| Total number of polymer chains | 2 |
| Total formula weight | 41458.84 |
| Authors | Maurus, R.,Brayer, G.D. (deposition date: 2008-12-04, release date: 2009-01-27, Last modification date: 2024-11-27) |
| Primary citation | Dalal, K.,Nguyen, N.,Alami, M.,Tan, J.,Moraes, T.F.,Lee, W.C.,Maurus, R.,Sligar, S.S.,Brayer, G.D.,Duong, F. Structure, Binding, and Activity of Syd, a SecY-interacting Protein J.Biol.Chem., 284:7897-7902, 2009 Cited by PubMed Abstract: The Syd protein has been implicated in the Sec-dependent transport of polypeptides across the bacterial inner membrane. Using Nanodiscs, we here provide direct evidence that Syd binds the SecY complex, and we demonstrate that interaction involves the two electropositive and cytosolic loops of the SecY subunit. We solve the crystal structure of Syd and together with cysteine cross-link analysis, we show that a conserved concave and electronegative groove constitutes the SecY-binding site. At the membrane, Syd decreases the activity of the translocon containing loosely associated SecY-SecE subunits, whereas in detergent solution Syd disrupts the SecYEG heterotrimeric associations. These results support the role of Syd in proofreading the SecY complex biogenesis and point to the electrostatic nature of the Sec channel interaction with its cytosolic partners. PubMed: 19139097DOI: 10.1074/jbc.M808305200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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