5XZ0
Staphylococcal Enterotoxin B (SEB) mutant S19 - N23A, Y90A, R110A and F177A
Summary for 5XZ0
Entry DOI | 10.2210/pdb5xz0/pdb |
Descriptor | Staphylococcal enterotoxin B (2 entities in total) |
Functional Keywords | staphylococcal aureus, enterotoxin, seb, toxin |
Biological source | Staphylococcus aureus (strain COL) |
Total number of polymer chains | 2 |
Total formula weight | 55194.16 |
Authors | Jeong, W.H.,Song, D.H.,Hur, G.H.,Jeong, S.T. (deposition date: 2017-07-11, release date: 2017-11-01, Last modification date: 2024-10-09) |
Primary citation | Jeong, W.H.,Song, D.H.,Hur, G.H.,Jeong, S.T. Structure of the staphylococcal enterotoxin B vaccine candidate S19 showing eliminated superantigen activity Acta Crystallogr F Struct Biol Commun, 73:595-600, 2017 Cited by PubMed Abstract: Four mutations (N23A, Y90A, R110A and F177A) were introduced into S19, a vaccine candidate for staphylococcal enterotoxin B (SEB), resulting in a lower binding affinity towards the T-cell receptor beta chain (TCB) and reducing its superantigen activity. The structure of S19 was solved and was superposed on the native or complex structure of SEB. In the superposition model, mutations that were introduced seemed to reduce the number of hydrogen bonds at the SEB-TCB interface. S19 also displayed an unexpected structural change around the flexible-loop region owing to the Y90A mutation. This local structural change provided evidence that the mutated form of S19 could have a lower affinity for major histocompatibility complex (MHC) class II than wild-type SEB. PubMed: 29095152DOI: 10.1107/S2053230X17014844 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.002 Å) |
Structure validation
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