6LYJ
The crystal structure of SAUGI/EBVUDG complex
Summary for 6LYJ
| Entry DOI | 10.2210/pdb6lyj/pdb |
| Descriptor | Uracil-DNA glycosylase, SAUGI (3 entities in total) |
| Functional Keywords | dna mimic protein, uracil-dna glycosylase inhibitor, uracil-dna glycosylase, dna repair, herpesvirus, hydrolase |
| Biological source | Epstein-Barr virus (strain GD1) (HHV-4,Human herpesvirus 4,Human gammaherpesvirus 4) More |
| Total number of polymer chains | 4 |
| Total formula weight | 84018.35 |
| Authors | Liao, Y.T.,Ko, T.P.,Wang, H.C. (deposition date: 2020-02-14, release date: 2020-06-24, Last modification date: 2023-11-29) |
| Primary citation | Liao, Y.T.,Lin, S.J.,Ko, T.P.,Liu, C.Y.,Hsu, K.C.,Wang, H.C. Structural insight into the differential interactions between the DNA mimic protein SAUGI and two gamma herpesvirus uracil-DNA glycosylases. Int.J.Biol.Macromol., 160:903-914, 2020 Cited by PubMed Abstract: Uracil-DNA glycosylases (UDGs) are conserved DNA-repair enzymes that can be found in many species, including herpesviruses. Since they play crucial roles for efficient viral DNA replication in herpesviruses, they have been considered as potential antiviral targets. In our previous work, Staphylococcus aureus SAUGI was identified as a DNA mimic protein that targets UDGs from S. aureus, human, Herpes simplex virus (HSV) and Epstein-Barr virus (EBV). Interestingly, SAUGI has the strongest inhibitory effects with EBVUDG. Here, we determined complex structures of SAUGI with EBVUDG and another γ-herpesvirus UDG from Kaposi's sarcoma-associated herpesvirus (KSHVUDG), which SAUGI fails to effectively inhibit. Structural analysis of the SAUGI/EBVUDG complex suggests that the additional interaction between SAUGI and the leucine loop may explain why SAUGI shows the highest binding capacity with EBVUDG. In contrast, SAUGI appears to make only partial contacts with the key components responsible for the compression and stabilization of the DNA backbone in the leucine loop extension of KSHVUDG. The findings in this study provide a molecular explanation for the differential inhibitory effects and binding strengths that SAUGI has on these two UDGs, and the structural basis of the differences should be helpful in developing inhibitors that would interfere with viral DNA replication. PubMed: 32502608DOI: 10.1016/j.ijbiomac.2020.05.267 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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