Structure of Toxic Shock Syndrome Toxin 1

G. Sridhar Prasad; Cathleen A. Earhart; Debra L. Murray; Richard P. Novick; Patrick M. Schlievert; Douglas H. Ohlendorf

doi:10.1021/bi00213a001

Structure of Toxic Shock Syndrome Toxin 1

G. Sridhar Prasad, Cathleen A. Earhart, Debra L. Murray, Richard P. Novick, Patrick M. Schlievert, Douglas H. Ohlendorf

Chemical and Structural Biology (TMED)

Research output: Contribution to journal › Article › peer-review

114 Scopus citations

Abstract

The three-dimensional structure of toxic shock syndrome toxin 1 (TSST-1) from Staphylococcus aureus has been determined and refined to an R value of 0.226 for data between 8- and 2.5-Å resolution. Overall, the structure of TSST-1 is similar to that of another superantigen, staphylococcal enterotoxin B (SEB). The key differences between these molecules are in the amino termini and in the degree to which a long central helix is covered by surface loops. The region around the carboxyl end of this central helix is proposed to govern the superantigenic properties of TSST-1. An adjacent region along this helix is proposed to be critical in the ability of TSST-1 to induce toxic shock syndrome.

Original language	English (US)
Pages (from-to)	13761-13766
Number of pages	6
Journal	Biochemistry
Volume	32
Issue number	50
DOIs	https://doi.org/10.1021/bi00213a001
State	Published - Dec 21 1993

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title = "Structure of Toxic Shock Syndrome Toxin 1",

abstract = "The three-dimensional structure of toxic shock syndrome toxin 1 (TSST-1) from Staphylococcus aureus has been determined and refined to an R value of 0.226 for data between 8- and 2.5-{\AA} resolution. Overall, the structure of TSST-1 is similar to that of another superantigen, staphylococcal enterotoxin B (SEB). The key differences between these molecules are in the amino termini and in the degree to which a long central helix is covered by surface loops. The region around the carboxyl end of this central helix is proposed to govern the superantigenic properties of TSST-1. An adjacent region along this helix is proposed to be critical in the ability of TSST-1 to induce toxic shock syndrome.",

author = "Prasad, {G. Sridhar} and Earhart, {Cathleen A.} and Murray, {Debra L.} and Novick, {Richard P.} and Schlievert, {Patrick M.} and Ohlendorf, {Douglas H.}",

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doi = "10.1021/bi00213a001",

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TY - JOUR

T1 - Structure of Toxic Shock Syndrome Toxin 1

AU - Prasad, G. Sridhar

AU - Earhart, Cathleen A.

AU - Murray, Debra L.

AU - Novick, Richard P.

AU - Schlievert, Patrick M.

AU - Ohlendorf, Douglas H.

PY - 1993/12/21

Y1 - 1993/12/21

N2 - The three-dimensional structure of toxic shock syndrome toxin 1 (TSST-1) from Staphylococcus aureus has been determined and refined to an R value of 0.226 for data between 8- and 2.5-Å resolution. Overall, the structure of TSST-1 is similar to that of another superantigen, staphylococcal enterotoxin B (SEB). The key differences between these molecules are in the amino termini and in the degree to which a long central helix is covered by surface loops. The region around the carboxyl end of this central helix is proposed to govern the superantigenic properties of TSST-1. An adjacent region along this helix is proposed to be critical in the ability of TSST-1 to induce toxic shock syndrome.

AB - The three-dimensional structure of toxic shock syndrome toxin 1 (TSST-1) from Staphylococcus aureus has been determined and refined to an R value of 0.226 for data between 8- and 2.5-Å resolution. Overall, the structure of TSST-1 is similar to that of another superantigen, staphylococcal enterotoxin B (SEB). The key differences between these molecules are in the amino termini and in the degree to which a long central helix is covered by surface loops. The region around the carboxyl end of this central helix is proposed to govern the superantigenic properties of TSST-1. An adjacent region along this helix is proposed to be critical in the ability of TSST-1 to induce toxic shock syndrome.

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JO - Biochemistry

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Structure of Toxic Shock Syndrome Toxin 1

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