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PDBsum entry 5tss

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Toxin PDB id
5tss
Contents
Protein chains
194 a.a. *
Waters ×27
* Residue conservation analysis

References listed in PDB file
Key reference
Title Refined structures of three crystal forms of toxic shock syndrome toxin-1 and of a tetramutant with reduced activity.
Authors G.S.Prasad, R.Radhakrishnan, D.T.Mitchell, C.A.Earhart, M.M.Dinges, W.J.Cook, P.M.Schlievert, D.H.Ohlendorf.
Ref. Protein Sci, 1997, 6, 1220-1227. [DOI no: 10.1002/pro.5560060610]
PubMed id 9194182
Abstract
The structure of toxic shock syndrome toxin-1 (TSST-1), the causative agent in toxic shock syndrome, has been determined in three crystal forms. The three structural models have been refined to R-factors of 0.154, 0.150, and 0.198 at resolutions of 2.05 A, 2.90 A, and 2.75 A, respectively. One crystal form of TSST-1 contains a zinc ion bound between two symmetry-related molecules. Although not required for biological activity, zinc dramatically potentiates the mitogenicity of TSST-1 at very low concentrations. In addition, the structure of the tetramutant TSST-1H [T69I, Y80W, E132K, I140T], which is nonmitogenic and does not amplify endotoxin shock, has been determined and refined in a fourth crystal form (R-factor = 0.173 to 1.9 A resolution).
Figure 1.
Fig. 1. Front view of TSST-I Numbers refer to /3 strands: letters refer to helices. Key structural features are shown extracted from the rest of the molecule.
Figure 2.
Fig. 2. 2F, - F, electrondensitymapscontouredat I n. (A) RegionaroundPhe 131 in C2221 crystal form. Thesidechainbeyond Cg was mittedfromthepositionalrefinementandphasecalculation. (B) Regionaround Zn 206 in P4,2)2 crystalform.Symmetry- relatedmolecule is gray.
The above figures are reprinted from an Open Access publication published by the Protein Society: Protein Sci (1997, 6, 1220-1227) copyright 1997.
Secondary reference #1
Title Structure of toxic shock syndrome toxin 1.
Authors G.S.Prasad, C.A.Earhart, D.L.Murray, R.P.Novick, P.M.Schlievert, D.H.Ohlendorf.
Ref. Biochemistry, 1993, 32, 13761-13766. [DOI no: 10.1021/bi00213a001]
PubMed id 8268150
Full text Abstract
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