This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1uns

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 06:26, 10 September 2015

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

Structural highlights

1uns is a 1 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1cqv, 1i4p, 1i4q, 1i4r, 1i4x, 1se2, 1ste
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[ENTC2_STAAU] Staphylococcal enterotoxins cause the intoxication staphylococcal food poisoning syndrome. The illness characterized by high fever, hypotension, diarrhea, shock, and in some cases death.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Papageorgiou AC, Baker MD, McLeod JD, Goda SK, Manzotti CN, Sansom DM, Tranter HS, Acharya KR. Identification of a secondary zinc-binding site in staphylococcal enterotoxin C2. Implications for superantigen recognition. J Biol Chem. 2004 Jan 9;279(2):1297-303. Epub 2003 Oct 14. PMID:14559915 doi:10.1074/jbc.M307333200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1uns"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cqv|1cqv]], [[1i4p|1i4p]], [[1i4q|1i4q]], [[1i4r|1i4r]], [[1i4x|1i4x]], [[1se2|1se2]], [[1ste|1ste]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uns OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1uns RCSB], [http://www.ebi.ac.uk/pdbsum/1uns PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uns OCA], [http://pdbe.org/1uns PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uns RCSB], [http://www.ebi.ac.uk/pdbsum/1uns PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/ENTC2_STAAU ENTC2_STAAU]] Staphylococcal enterotoxins cause the intoxication staphylococcal food poisoning syndrome. The illness characterized by high fever, hypotension, diarrhea, shock, and in some cases death.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 25: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1uns" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1uns

From Proteopedia

Revision as of 06:26, 10 September 2015

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox