1DYQ

STAPHYLOCOCCAL ENTEROTOXIN A MUTANT VACCINE

Summary for 1DYQ

• Entry DOI: 10.2210/pdb1dyq/pdb
• Related: 1ESF 1SEA 1SXT
• Descriptor: Enterotoxin type A, ZINC ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: enterotoxin, staphylococcal enterotoxin type a, vaccine
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 1
• Total formula weight: 27417.02

Authors

Krupka, H.I.,Segelke, B.W.,Rupp, B. (deposition date: 2000-02-05, release date: 2001-03-19, Last modification date: 2024-11-13)

Primary citation

Krupka, H.I.,Segelke, B.W.,Ulrich, R.,Ringhofer, S.,Knapp, M.,Rupp, B.
Structural Basis for Abrogated Binding between Staphylococcal Enterotoxin a Superantigen Vaccine and Mhc-II?
Protein Sci., 11:642-, 2002

PubMed Abstract: Staphylococcal enterotoxins (SEs) are superantigenic protein toxins responsible for a number of life-threatening diseases. The X-ray structure of a staphylococcal enterotoxin A (SEA) triple-mutant (L48R, D70R, and Y92A) vaccine reveals a cascade of structural rearrangements located in three loop regions essential for binding the alpha subunit of major histocompatibility complex class II (MHC-II) molecules. A comparison of hypothetical model complexes between SEA and the SEA triple mutant with MHC-II HLA-DR1 clearly shows disruption of key ionic and hydrophobic interactions necessary for forming the complex. Extensive dislocation of the disulfide loop in particular interferes with MHC-IIalpha binding. The triple-mutant structure provides new insights into the loss of superantigenicity and toxicity of an engineered superantigen and provides a basis for further design of enterotoxin vaccines.

PubMed: 11847286
DOI: 10.1110/PS.39702

Experimental method

X-RAY DIFFRACTION (1.5 Å)