5OED
Human Rab32:GDP in complex with Salmonella GtgE C45A mutant
Summary for 5OED
| Entry DOI | 10.2210/pdb5oed/pdb |
| Related | 4CYM 4MI7 |
| Descriptor | GtgE, Ras-related protein Rab-32, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | rab gtpase, posttranslational modification, proteolysis, salmonella infection, hydrolase |
| Biological source | Salmonella choleraesuis More |
| Cellular location | Mitochondrion : Q13637 |
| Total number of polymer chains | 2 |
| Total formula weight | 47726.66 |
| Authors | Wachtel, R.,Braeuning, B.,Mader, S.L.,Ecker, F.,Kaila, V.R.I.,Groll, M.,Itzen, A. (deposition date: 2017-07-07, release date: 2018-01-10, Last modification date: 2024-01-17) |
| Primary citation | Wachtel, R.,Brauning, B.,Mader, S.L.,Ecker, F.,Kaila, V.R.I.,Groll, M.,Itzen, A. The protease GtgE from Salmonella exclusively targets inactive Rab GTPases. Nat Commun, 9:44-44, 2018 Cited by PubMed Abstract: Salmonella infections require the delivery of bacterial effectors into the host cell that alter the regulation of host defense mechanisms. The secreted cysteine protease GtgE from S. Typhimurium manipulates vesicular trafficking by modifying the Rab32 subfamily via cleaving the regulatory switch I region. Here we present a comprehensive biochemical, structural, and computational characterization of GtgE in complex with Rab32. Interestingly, GtgE solely processes the inactive GDP-bound GTPase. The crystal structure of the Rab32:GDP substrate in complex with the inactive mutant GtgE reveals the molecular basis of substrate recognition. In combination with atomistic molecular dynamics simulations, the structural determinants for protein and activity-state specificity are identified. Mutations in a central interaction hub lead to loss of the strict GDP specificity. Our findings shed light on the sequence of host cell manipulation events during Salmonella infection and provide an explanation for the dependence on the co-secreted GTPase activating protein SopD2. PubMed: 29298974DOI: 10.1038/s41467-017-02110-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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