5E9T
Crystal structure of GtfA/B complex
Summary for 5E9T
| Entry DOI | 10.2210/pdb5e9t/pdb |
| Related | 5E9U |
| Descriptor | Glycosyltransferase Gtf1, Glycosyltransferase-stabilizing protein Gtf2, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | glycosyltransferase, accessory protein translocation, complex, transferase-chaperone complex, transferase/chaperone |
| Biological source | Streptococcus gordonii More |
| Total number of polymer chains | 4 |
| Total formula weight | 220118.67 |
| Authors | Chen, Y.,Rapoport, T.A. (deposition date: 2015-10-15, release date: 2016-03-02, Last modification date: 2024-10-16) |
| Primary citation | Chen, Y.,Seepersaud, R.,Bensing, B.A.,Sullam, P.M.,Rapoport, T.A. Mechanism of a cytosolic O-glycosyltransferase essential for the synthesis of a bacterial adhesion protein. Proc.Natl.Acad.Sci.USA, 113:E1190-E1199, 2016 Cited by PubMed Abstract: O-glycosylation of Ser and Thr residues is an important process in all organisms, which is only poorly understood. Such modification is required for the export and function of adhesin proteins that mediate the attachment of pathogenic Gram-positive bacteria to host cells. Here, we have analyzed the mechanism by which the cytosolic O-glycosyltransferase GtfA/B of Streptococcus gordonii modifies the Ser/Thr-rich repeats of adhesin. The enzyme is a tetramer containing two molecules each of GtfA and GtfB. The two subunits have the same fold, but only GtfA contains an active site, whereas GtfB provides the primary binding site for adhesin. During a first phase of glycosylation, the conformation of GtfB is restrained by GtfA to bind substrate with unmodified Ser/Thr residues. In a slow second phase, GtfB recognizes residues that are already modified with N-acetylglucosamine, likely by converting into a relaxed conformation in which one interface with GtfA is broken. These results explain how the glycosyltransferase modifies a progressively changing substrate molecule. PubMed: 26884191DOI: 10.1073/pnas.1600494113 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.92 Å) |
Structure validation
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