1uns

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==Overview==
==Overview==
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The previously determined crystal structure of the superantigen, staphylococcal enterotoxin C2 (SEC2) showed binding of a single zinc ion, located between the N- and C-terminal domains. Here we present the crystal, structure of SEC2 determined to 2.0 A resolution in the presence of, additional zinc. The structure revealed the presence of a secondary, zinc-binding site close to the major histocompatibility complex, (MHC)-binding site of the toxin and some 28 A away from the primary, zinc-binding site of the toxin found in previous studies. T cell, stimulation assays showed that varying the concentration of zinc ions, present affected the activity of the toxin and we observed that high zinc, concentrations considerably inhibited T cell responses. This indicates, that SEC2 may have multiple modes of interaction with the immune system, that are dependent on serum zinc levels. The potential role of the, secondary zinc-binding site and that of the primary one in the formation, of the TCR.SEC2.MHC complex are considered, and the possibility that zinc, may regulate the activity of SEC2 as a toxin facilitating different T cell, responses is discussed.
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The previously determined crystal structure of the superantigen staphylococcal enterotoxin C2 (SEC2) showed binding of a single zinc ion located between the N- and C-terminal domains. Here we present the crystal structure of SEC2 determined to 2.0 A resolution in the presence of additional zinc. The structure revealed the presence of a secondary zinc-binding site close to the major histocompatibility complex (MHC)-binding site of the toxin and some 28 A away from the primary zinc-binding site of the toxin found in previous studies. T cell stimulation assays showed that varying the concentration of zinc ions present affected the activity of the toxin and we observed that high zinc concentrations considerably inhibited T cell responses. This indicates that SEC2 may have multiple modes of interaction with the immune system that are dependent on serum zinc levels. The potential role of the secondary zinc-binding site and that of the primary one in the formation of the TCR.SEC2.MHC complex are considered, and the possibility that zinc may regulate the activity of SEC2 as a toxin facilitating different T cell responses is discussed.
==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
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[[Category: Acharya, K.R.]]
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[[Category: Acharya, K R.]]
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[[Category: Baker, M.D.]]
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[[Category: Baker, M D.]]
[[Category: Goda, S.]]
[[Category: Goda, S.]]
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[[Category: Mcleod, J.D.]]
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[[Category: Mcleod, J D.]]
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[[Category: Papageorgiou, A.C.]]
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[[Category: Papageorgiou, A C.]]
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[[Category: Sansom, D.M.]]
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[[Category: Sansom, D M.]]
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[[Category: Tranter, H.S.]]
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[[Category: Tranter, H S.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: enterotoxin]]
[[Category: enterotoxin]]
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[[Category: zinc-binding site]]
[[Category: zinc-binding site]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:03:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:26:30 2008''

Revision as of 13:26, 21 February 2008


1uns, resolution 2.0Å

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IDENTIFICATION OF A SECONDARY ZINC-BINDING SITE IN STAPHYLOCOCCAL ENTEROTOXIN C2: IMPLICATIONS FOR SUPERANTIGEN RECOGNITION

Overview

The previously determined crystal structure of the superantigen staphylococcal enterotoxin C2 (SEC2) showed binding of a single zinc ion located between the N- and C-terminal domains. Here we present the crystal structure of SEC2 determined to 2.0 A resolution in the presence of additional zinc. The structure revealed the presence of a secondary zinc-binding site close to the major histocompatibility complex (MHC)-binding site of the toxin and some 28 A away from the primary zinc-binding site of the toxin found in previous studies. T cell stimulation assays showed that varying the concentration of zinc ions present affected the activity of the toxin and we observed that high zinc concentrations considerably inhibited T cell responses. This indicates that SEC2 may have multiple modes of interaction with the immune system that are dependent on serum zinc levels. The potential role of the secondary zinc-binding site and that of the primary one in the formation of the TCR.SEC2.MHC complex are considered, and the possibility that zinc may regulate the activity of SEC2 as a toxin facilitating different T cell responses is discussed.

About this Structure

1UNS is a Single protein structure of sequence from Staphylococcus aureus with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Identification of a secondary zinc-binding site in staphylococcal enterotoxin C2. Implications for superantigen recognition., Papageorgiou AC, Baker MD, McLeod JD, Goda SK, Manzotti CN, Sansom DM, Tranter HS, Acharya KR, J Biol Chem. 2004 Jan 9;279(2):1297-303. Epub 2003 Oct 14. PMID:14559915

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