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5XZ0

Staphylococcal Enterotoxin B (SEB) mutant S19 - N23A, Y90A, R110A and F177A

Summary for 5XZ0
Entry DOI10.2210/pdb5xz0/pdb
DescriptorStaphylococcal enterotoxin B (2 entities in total)
Functional Keywordsstaphylococcal aureus, enterotoxin, seb, toxin
Biological sourceStaphylococcus aureus (strain COL)
Total number of polymer chains2
Total formula weight55194.16
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 citationJeong, 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: 29095152
DOI: 10.1107/S2053230X17014844
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.002 Å)
Structure validation

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