Structure of IDP90224
Structure of the type III effector/phosphothreonine lyase OspF from Shigella flexneri
- CSGID target
- IDP90224
- PDB Id
- 3I0U (NCBI MMDB)
- Authors
- Singer A.U., Skarina T., Nocek B., Gordon R., Lam R., Kagan O., Edwards A.M., Joachimiak A., Chirgadze N.Y., Anderson W.F., Savchenko A., Center for Structural Genomics of Infectious Diseases (CSGID)
- Responsible person
- Alexander Singer
- Responsible lab
- University of Toronto
- Deposition Date
- 2009-06-25
- Release Date
- 2009-09-01
Annotation
- Description
- Gram-negative pathogens exert virulence to a significant degree by the secretion of toxins, termed effectors, through the type III secretion system. One effector from Salmonella sp., SpvC, was found to have a highly novel enzymatic function, irreversibly dephosphorylating an activating threonine residue on MAP kinase proteins via a lyase activity (phosphothreonine lyase), leaving a double bond between the alpha and beta carbon (Science. 2007 315:1000-3.). We have solved the structure of the homologue of SpvC from Shigella flexneri, termed OspF, to 2.7 Å, from residue 23 to the C-terminus. This structure shows a very similar overall fold to Salmonella enterica SpvC, to which it shares 64% sequence identity. The principal difference involves a change in direction in the most N-terminal helix, which folds around the structure in SpvC but which remains straight in OspF. The overall significance of this finding has yet to be determined. Although 2 molecules of OspF can be found in an asymmetric unit in crystals, the protein is predicted to be monomeric.
- Functional assignment
- phosphothreonince lyase
Ligands
| Ligand code | Name | Ligand type |
|---|---|---|
| MPD | (4S)-2-methyl-2,4-pentanediol | crystallization |
Structure information
Unit cell parameters
- Space Group
- P 41 21 2
- Unit Cell
-
a=62.13Å, b=62.13Å, c=239.59Å
α=90.00, β=90.00, γ=90.00 - Solvent content
- Matthews coefficient
- Resolution range
- 43.94-2.70Å (2.77-2.70Å)
- Rall(%)
- 25.2
- Rwork(%)
- 25.0 (26.4)
- Rfree(%)
- 28.7 (33.3)
- Num. observed reflections
- 13700 (963)
- Num. Rfree reflections
- 671 (43)
- Completeness(%)
- 99.8 (100.0)
- Num Atoms
- 3207
- Num Waters
- 6
- Num Hetatoms
- 8
- Model mean isotropic B factor
- 71.020Å2
- RMSD bond length
- 0.017Å
- RMSD bond angle
- 1.713°
- Filename uploaded
- rcsb053822_final.pdb (uploaded on 2009-10-05 11:47:57-04)
