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1f77

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Revision as of 09:32, 27 December 2017

STAPHYLOCOCCAL ENTEROTOXIN H DETERMINED TO 2.4 A RESOLUTION

Structural highlights

1f77 is a 2 chain structure with sequence from "micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1enf, 1ewz
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ETXH_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 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.

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^[1]

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

References

↑ Hakansson M, Petersson K, Nilsson H, Forsberg G, Bjork P, Antonsson P, Svensson LA. The crystal structure of staphylococcal enterotoxin H: implications for binding properties to MHC class II and TcR molecules. J Mol Biol. 2000 Sep 22;302(3):527-37. PMID:10986116 doi:http://dx.doi.org/10.1006/jmbi.2000.4093

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/1f77"

@@ Line 1: / Line 1: @@
 ==STAPHYLOCOCCAL ENTEROTOXIN H DETERMINED TO 2.4 A RESOLUTION==
 <StructureSection load='1f77' size='340' side='right' caption='[[1f77]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1enf|1enf]], [[1ewz|1ewz]]</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=1f77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f77 OCA], [http://pdbe.org/1f77 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f77 RCSB], [http://www.ebi.ac.uk/pdbsum/1f77 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=1f77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f77 OCA], [http://pdbe.org/1f77 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f77 RCSB], [http://www.ebi.ac.uk/pdbsum/1f77 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1f77 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f7/1f77_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f7/1f77_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1f77

From Proteopedia

Revision as of 09:32, 27 December 2017

STAPHYLOCOCCAL ENTEROTOXIN H DETERMINED TO 2.4 A RESOLUTION

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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