5WXK
EarP bound with domain I of EF-P
Summary for 5WXK
| Entry DOI | 10.2210/pdb5wxk/pdb |
| Related | 5WXI 5WXJ |
| Descriptor | EarP, Elongation factor P, THYMIDINE-5'-DIPHOSPHATE, ... (8 entities in total) |
| Functional Keywords | glycosyltransferase, gt-b, ef-p, rhamnosylation, translation elongation, dtdp-rhamnose, transferase |
| Biological source | Neisseria meningitidis serogroup B / serotype 15 (strain H44/76) More |
| Cellular location | Cytoplasm : E6MVW0 |
| Total number of polymer chains | 2 |
| Total formula weight | 53261.65 |
| Authors | Sengoku, T.,Yokoyama, S.,Yanagisawa, T. (deposition date: 2017-01-07, release date: 2018-02-28, Last modification date: 2024-04-03) |
| Primary citation | Sengoku, T.,Suzuki, T.,Dohmae, N.,Watanabe, C.,Honma, T.,Hikida, Y.,Yamaguchi, Y.,Takahashi, H.,Yokoyama, S.,Yanagisawa, T. Structural basis of protein arginine rhamnosylation by glycosyltransferase EarP Nat. Chem. Biol., 14:368-374, 2018 Cited by PubMed Abstract: Protein glycosylation regulates many cellular processes. Numerous glycosyltransferases with broad substrate specificities have been structurally characterized. A novel inverting glycosyltransferase, EarP, specifically transfers rhamnose from dTDP-β-L-rhamnose to Arg32 of bacterial translation elongation factor P (EF-P) to activate its function. Here we report a crystallographic study of Neisseria meningitidis EarP. The EarP structure contains two tandem Rossmann-fold domains, which classifies EarP in glycosyltransferase superfamily B. In contrast to other structurally characterized protein glycosyltransferases, EarP binds the entire β-sheet structure of EF-P domain I through numerous interactions that specifically recognize its conserved residues. Thus Arg32 is properly located at the active site, and causes structural change in a conserved dTDP-β-L-rhamnose-binding loop of EarP. Rhamnosylation by EarP should occur via an S2 reaction, with Asp20 as the general base. The Arg32 binding and accompanying structural change of EarP may induce a change in the rhamnose-ring conformation suitable for the reaction. PubMed: 29440735DOI: 10.1038/s41589-018-0002-y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.801 Å) |
Structure validation
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