3L3P
Crystal structure of the C-terminal domain of Shigella type III effector IpaH9.8, with a novel domain swap
Summary for 3L3P
| Entry DOI | 10.2210/pdb3l3p/pdb |
| Related | 3ckd 3cvr |
| Descriptor | IpaH9.8 (1 entity in total) |
| Functional Keywords | e3 ligase, domain swap, cxd motif, ligase |
| Biological source | Shigella flexneri |
| Total number of polymer chains | 1 |
| Total formula weight | 33460.03 |
| Authors | Seyedarabi, A.,Sullivan, J.A.,Sasakawa, C.,Pickersgill, R.W. (deposition date: 2009-12-17, release date: 2010-09-08, Last modification date: 2023-11-01) |
| Primary citation | Seyedarabi, A.,Sullivan, J.A.,Sasakawa, C.,Pickersgill, R.W. A disulfide driven domain swap switches off the activity of Shigella IpaH9.8 E3 ligase Febs Lett., 584:4163-4168, 2010 Cited by PubMed Abstract: We show that the monomeric form of Shigella IpaH9.8 E3 ligase catalyses the ubiquitination of human U2AF35 in vitro, providing a molecular mechanism for the observed in vivo effect. We further discover that under non-reducing conditions IpaH9.8 undergoes a domain swap driven by the formation of a disulfide bridge involving the catalytic cysteine and that this dimer is unable to catalyse the ubiquitination of U2AF35. The crystal structure of the domain-swapped dimer is presented. The redox inactivation of IpaH9.8 could be a mechanism of regulating the activity of the IpaH9.8 E3 ligase in response to cell damage so that the host cell in which the bacteria resides is maintained in a benign state suitable for bacterial survival. PubMed: 20831869DOI: 10.1016/j.febslet.2010.09.006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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