5AYS
Crystal structure of SAUGI/HSV UDG complex
Summary for 5AYS
| Entry DOI | 10.2210/pdb5ays/pdb |
| Related | 5AYR |
| Descriptor | Uracil-DNA glycosylase, Uncharacterized protein (3 entities in total) |
| Functional Keywords | dna mimic protein, dna mimicking, uracil-dna glycosylase inhibitor, uracil-dna glycosylase, herpes simplex virus, hydrolase inhibitor |
| Biological source | Human herpesvirus 1 (strain 17) (HHV-1) More |
| Total number of polymer chains | 4 |
| Total formula weight | 84578.52 |
| Authors | Wang, H.C.,Ko, T.P.,Huang, M.F.,Wang, A.H.J. (deposition date: 2015-09-02, release date: 2016-06-08, Last modification date: 2023-11-08) |
| Primary citation | Wang, H.C.,Ho, C.H.,Chou, C.C.,Ko, T.P.,Huang, M.F.,Hsu, K.C.,Wang, A.H. Using structural-based protein engineering to modulate the differential inhibition effects of SAUGI on human and HSV uracil DNA glycosylase. Nucleic Acids Res., 44:4440-4449, 2016 Cited by PubMed Abstract: Uracil-DNA glycosylases (UDGs) are highly conserved proteins that can be found in a wide range of organisms, and are involved in the DNA repair and host defense systems. UDG activity is controlled by various cellular factors, including the uracil-DNA glycosylase inhibitors, which are DNA mimic proteins that prevent the DNA binding sites of UDGs from interacting with their DNA substrate. To date, only three uracil-DNA glycosylase inhibitors, phage UGI, p56, and Staphylococcus aureus SAUGI, have been determined. We show here that SAUGI has differential inhibitory effects on UDGs from human, bacteria, Herpes simplex virus (HSV; human herpesvirus 1) and Epstein-Barr virus (EBV; human herpesvirus 4). Newly determined crystal structures of SAUGI/human UDG and a SAUGI/HSVUDG complex were used to explain the differential binding activities of SAUGI on these two UDGs. Structural-based protein engineering was further used to modulate the inhibitory ability of SAUGI on human UDG and HSVUDG. The results of this work extend our understanding of DNA mimics as well as potentially opening the way for novel therapeutic applications for this kind of protein. PubMed: 26980279DOI: 10.1093/nar/gkw185 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.09 Å) |
Structure validation
Download full validation report
