3OEO
The crystal structure E. coli Spy
Summary for 3OEO
| Entry DOI | 10.2210/pdb3oeo/pdb |
| Related | 3OEJ |
| Descriptor | Spheroplast protein Y, CADMIUM ION (3 entities in total) |
| Functional Keywords | ltxxq, extracytoplasmic stress response-related, signaling protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 4 |
| Total formula weight | 66218.56 |
| Authors | Kwon, E.,Kim, D.Y.,Gross, C.A.,Gross, J.D.,Kim, K.K. (deposition date: 2010-08-13, release date: 2010-09-22, Last modification date: 2024-02-21) |
| Primary citation | Kwon, E.,Kim, D.Y.,Gross, C.A.,Gross, J.D.,Kim, K.K. The crystal structure Escherichia coli Spy. Protein Sci., 19:2252-2259, 2010 Cited by PubMed Abstract: Escherichia coli spheroplast protein y (EcSpy) is a small periplasmic protein that is homologous with CpxP, an inhibitor of the extracytoplasmic stress response. Stress conditions such as spheroplast formation induce the expression of Spy via the Cpx or the Bae two-component systems in E. coli, though the function of Spy is unknown. Here, we report the crystal structure of EcSpy, which reveals a long kinked hairpin-like structure of four α-helices that form an antiparallel dimer. The dimer contains a curved oval shape with a highly positively charged concave surface that may function as a ligand binding site. Sequence analysis reveals that Spy is highly conserved over the Enterobacteriaceae family. Notably, three conserved regions that contain identical residues and two LTxxQ motifs are placed at the horizontal end of the dimer structure, stabilizing the overall fold. CpxP also contains the conserved sequence motifs and has a predicted secondary structure similar to Spy, suggesting that Spy and CpxP likely share the same fold. PubMed: 20799348DOI: 10.1002/pro.489 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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