4BWR
Crystal structure of c5321: a protective antigen present in uropathogenic Escherichia coli strains displaying an SLR fold
Replaces: 2XM6Summary for 4BWR
| Entry DOI | 10.2210/pdb4bwr/pdb |
| Descriptor | PROTEIN CORRESPONDING TO LOCUS C5321 FROM CFT073 E.COLI STRAIN, MAGNESIUM ION, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | unknown function, sel1-like repeat, super-helical fold |
| Biological source | ESCHERICHIA COLI |
| Total number of polymer chains | 1 |
| Total formula weight | 54902.52 |
| Authors | Urosev, D.,Ferrer-Navarro, M.,Pastorello, I.,Cartocci, E.,Costenaro, L.,Zhulenkovs, D.,Marechal, J.-D.,Leonchiks, A.,Reverter, D.,Serino, L.,Soriani, M.,Daura, X. (deposition date: 2013-07-04, release date: 2013-07-24, Last modification date: 2024-11-20) |
| Primary citation | Urosev, D.,Ferrer-Navarro, M.,Pastorello, I.,Cartocci, E.,Costenaro, L.,Zhulenkovs, D.,Marechal, J.,Leonchiks, A.,Reverter, D.,Serino, L.,Soriani, M.,Daura, X. Crystal Structure of C5321: A Protective Antigen Present in Uropathogenic Escherichia Coli Strains Displaying an Slr Fold. Bmc Struct.Biol., 13:19-, 2013 Cited by PubMed Abstract: Increasing rates of antimicrobial resistance among uropathogens led, among other efforts, to the application of subtractive reverse vaccinology for the identification of antigens present in extraintestinal pathogenic E. coli (ExPEC) strains but absent or variable in non-pathogenic strains, in a quest for a broadly protective Escherichia coli vaccine. The protein coded by locus c5321 from CFT073 E. coli was identified as one of nine potential vaccine candidates against ExPEC and was able to confer protection with an efficacy of 33% in a mouse model of sepsis. c5321 (known also as EsiB) lacks functional annotation and structurally belongs to the Sel1-like repeat (SLR) family. Herein, as part of the general characterization of this potential antigen, we have focused on its structural properties. PubMed: 24099525DOI: 10.1186/1472-6807-13-19 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.74 Å) |
Structure validation
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