1TS4

Q139K MUTANT OF TOXIC SHOCK SYNDROME TOXIN-1 FROM S. AUREUS

Summary for 1TS4

• Entry DOI: 10.2210/pdb1ts4/pdb
• Descriptor: TOXIC SHOCK SYNDROME TOXIN-1 (1 entity in total)
• Functional Keywords: toxin, superantigen
• Biological source: Staphylococcus aureus
• Cellular location: Secreted: P06886
• Total number of polymer chains: 2
• Total formula weight: 44209.64

Authors

Earhart, C.A.,Mitchell, D.T.,Murray, D.L.,Pinheiro, D.M.,Matsumura, M.,Schlievert, P.M.,Ohlendorf, D.H. (deposition date: 1997-10-10, release date: 1998-12-16, Last modification date: 2024-05-22)

Primary citation

Earhart, C.A.,Mitchell, D.T.,Murray, D.L.,Pinheiro, D.M.,Matsumura, M.,Schlievert, P.M.,Ohlendorf, D.H.
Structures of five mutants of toxic shock syndrome toxin-1 with reduced biological activity.
Biochemistry, 37:7194-7202, 1998

PubMed Abstract: The three-dimensional structures of five mutants of toxic shock syndrome toxin-1 (TSST-1) have been determined. These mutations are in the long central alpha helix and are useful in mapping portions of TSST-1 involved in superantigenicity and lethality. The T128A, H135A, Q139K, and I140T mutations appear to reduce superantigenicity by altering the properties of the T-cell receptor interaction surface. The Q136A mutation is at a largely buried site and causes a dramatic change in the conformation of the beta7-beta9 loop which covers the back of the central alpha helix. As this mutation has the unique ability to reduce the toxin's lethality in rabbits while retaining its superantigenicity, it raises the possibility that this rear loop mediates the ability of TSST-1 to induce lethality and suggests a route for producing nonlethal toxins for therapeutic development.

PubMed: 9585531
DOI: 10.1021/bi9721896

Experimental method

X-RAY DIFFRACTION (3.4 Å)