1ewc
From Proteopedia
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| - | [[Image:1ewc.gif|left|200px]] | + | [[Image:1ewc.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF ZN2+ LOADED STAPHYLOCOCCAL ENTEROTOXIN H''' | + | {{Structure |
| + | |PDB= 1ewc |SIZE=350|CAPTION= <scene name='initialview01'>1ewc</scene>, resolution 1.95Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF ZN2+ LOADED STAPHYLOCOCCAL ENTEROTOXIN H''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EWC is a [ | + | 1EWC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EWC OCA]. |
==Reference== | ==Reference== | ||
| - | The crystal structure of staphylococcal enterotoxin H: implications for binding properties to MHC class II and TcR molecules., Hakansson M, Petersson K, Nilsson H, Forsberg G, Bjork P, Antonsson P, Svensson LA, J Mol Biol. 2000 Sep 22;302(3):527-37. PMID:[http:// | + | The crystal structure of staphylococcal enterotoxin H: implications for binding properties to MHC class II and TcR molecules., Hakansson M, Petersson K, Nilsson H, Forsberg G, Bjork P, Antonsson P, Svensson LA, J Mol Biol. 2000 Sep 22;302(3):527-37. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10986116 10986116] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
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[[Category: beta-grasp]] | [[Category: beta-grasp]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:01:07 2008'' |
Revision as of 09:01, 20 March 2008
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| , resolution 1.95Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF ZN2+ LOADED STAPHYLOCOCCAL ENTEROTOXIN H
Overview
The X-ray structure of the superantigen staphylococcal enterotoxin H (SEH) has been determined at 1.69 A resolution. In this paper we present two structures of zinc-free SEH (apoSEH) and one zinc-loaded form of SEH (ZnSEH). SEH exhibits the conventional superantigen (SAg) fold with two characteristic domains. In ZnSEH one zinc ion per SEH molecule is bound to the C-terminal beta-sheet in the region implicated for major histocompatibility complex class II (MHC class II) binding in SEA, SED and SEE. Surprisingly, the zinc ion has only two ligating amino acid residues His206 and Asp208. The other ligands to the zinc ion are two water molecules. An extensive packing interaction between two symmetry-related molecules in the crystal, 834 A(2)/molecule, forms a cavity that buries the zinc ions of the molecules. This dimer-like interaction is found in two crystal forms. Nevertheless, zinc-dependent dimerisation is not observed in solution, as seen in the case of SED. A unique feature of SEH as compared to other staphylococcal enterotoxins is a large negatively charged surface close to the Zn(2+) site. The interaction of SEH with MHC class II is the strongest known among the staphylococcal enterotoxins. However, SEH seems to lack a SEB-like MHC class II binding site, since the side-chain properties of structurally equivalent amino acid residues in SEH and those in SEB-binding MHC class II differ dramatically. There is also a structural flexibility between the domains of SEH. The domains of two apoSEH structures are related by a 5 degrees rotation leading to at most 3 A difference in C(alpha) positions. Since the T-cell receptor probably interacts with both domains, SEH by this rotation may modulate its binding to different TcR Vbeta-chains.
About this Structure
1EWC is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
The crystal structure of staphylococcal enterotoxin H: implications for binding properties to MHC class II and TcR molecules., Hakansson M, Petersson K, Nilsson H, Forsberg G, Bjork P, Antonsson P, Svensson LA, J Mol Biol. 2000 Sep 22;302(3):527-37. PMID:10986116
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