4BVU
Structure of Shigella effector OspG in complex with host UbcH5c- Ubiquitin conjugate
Summary for 4BVU
| Entry DOI | 10.2210/pdb4bvu/pdb |
| Descriptor | PROTEIN KINASE OSPG, UBIQUITIN-CONJUGATING ENZYME E2 D3, UBIQUITIN, ... (4 entities in total) |
| Functional Keywords | transferase-ligase-protein binding complex, kinase, transferase/ligase/protein binding |
| Biological source | SHIGELLA FLEXNERI More |
| Total number of polymer chains | 3 |
| Total formula weight | 49657.24 |
| Authors | Pruneda, J.N.,LeTrong, I.,Stenkamp, R.E.,Klevit, R.E.,Brzovic, P.S. (deposition date: 2013-06-28, release date: 2014-01-29, Last modification date: 2023-12-20) |
| Primary citation | Pruneda, J.N.,Smith, F.D.,Daurie, A.,Swaney, D.L.,Villen, J.,Scott, J.D.,Stadnyk, A.W.,Le Trong, I.,Stenkamp, R.E.,Klevit, R.E.,Rohde, J.R.,Brzovic, P.S. E2~Ub Conjugates Regulate the Kinase Activity of Shigella Effector Ospg During Pathogenesis. Embo J., 33:437-, 2014 Cited by PubMed Abstract: Pathogenic bacteria introduce effector proteins directly into the cytosol of eukaryotic cells to promote invasion and colonization. OspG, a Shigella spp. effector kinase, plays a role in this process by helping to suppress the host inflammatory response. OspG has been reported to bind host E2 ubiquitin-conjugating enzymes activated with ubiquitin (E2~Ub), a key enzyme complex in ubiquitin transfer pathways. A co-crystal structure of the OspG/UbcH5c~Ub complex reveals that complex formation has important ramifications for the activity of both OspG and the UbcH5c~Ub conjugate. OspG is a minimal kinase domain containing only essential elements required for catalysis. UbcH5c~Ub binding stabilizes an active conformation of the kinase, greatly enhancing OspG kinase activity. In contrast, interaction with OspG stabilizes an extended, less reactive form of UbcH5c~Ub. Recognizing conserved E2 features, OspG can interact with at least ten distinct human E2s~Ub. Mouse oral infection studies indicate that E2~Ub conjugates act as novel regulators of OspG effector kinase function in eukaryotic host cells. PubMed: 24446487DOI: 10.1002/EMBJ.201386386 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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