Summary for 1N5B
| Entry DOI | 10.2210/pdb1n5b/pdb |
| Related | 1JYA 1K6Z 1L2W 1MD1 |
| Descriptor | YOPE regulator (2 entities in total) |
| Functional Keywords | yersinia enterocolitica, molecular chaperone, type iii secretion system, chaperone |
| Biological source | Yersinia enterocolitica |
| Total number of polymer chains | 4 |
| Total formula weight | 59359.01 |
| Authors | Trame, C.B.,McKay, D.B. (deposition date: 2002-11-05, release date: 2002-11-20, Last modification date: 2024-02-14) |
| Primary citation | Trame, C.B.,McKay, D.B. Structure of the Yersinia enterocolitica molecular-chaperone protein SycE. Acta Crystallogr.,Sect.D, 59:389-392, 2003 Cited by PubMed Abstract: The crystal structure of the Yersinia enterocolitica molecular-chaperone protein SycE, which specifically binds the YopE protein, has been solved to 2.0 A resolution by molecular replacement. The crystal contains two SycE dimers per asymmetric unit; a novel feature of this crystal, when compared with closely related SycE structures, is a well ordered carboxy-terminal peptide in one protomer of each dimer. The peptide binds a hydrophobic patch of a neighboring molecule in a manner similar to that seen in a SycE-YopE chaperone-target complex, suggestive of low-affinity 'self-binding' through which the carboxy-terminal peptide might suppress counterproductive interactions with non-target proteins in vivo. PubMed: 12554962DOI: 10.1107/S0907444902020826 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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