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| <StructureSection load='1qoh' size='340' side='right'caption='[[1qoh]], [[Resolution|resolution]] 2.35Å' scene=''> | | <StructureSection load='1qoh' size='340' side='right'caption='[[1qoh]], [[Resolution|resolution]] 2.35Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[1qoh]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QOH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1qoh]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QOH FirstGlance]. <br> |
- | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bos|1bos]], [[1bov|1bov]], [[2bos|2bos]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35Å</td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qoh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qoh OCA], [https://pdbe.org/1qoh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qoh RCSB], [https://www.ebi.ac.uk/pdbsum/1qoh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qoh ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qoh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qoh OCA], [https://pdbe.org/1qoh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qoh RCSB], [https://www.ebi.ac.uk/pdbsum/1qoh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qoh ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/Q47644_ECOLX Q47644_ECOLX] |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | | |
| ==See Also== | | ==See Also== |
- | *[[Shiga toxin|Shiga toxin]] | + | *[[Shiga toxin 3D structures|Shiga toxin 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Armstrong, G D]] | + | [[Category: Armstrong GD]] |
- | [[Category: Boodhoo, A]] | + | [[Category: Boodhoo A]] |
- | [[Category: Brunton, J L]] | + | [[Category: Brunton JL]] |
- | [[Category: Clark, C G]] | + | [[Category: Clark CG]] |
- | [[Category: Pannu, N S]] | + | [[Category: Pannu NS]] |
- | [[Category: Read, R J]] | + | [[Category: Read RJ]] |
- | [[Category: Protein-carbohydrate recognition]]
| + | |
- | [[Category: Receptor binding]]
| + | |
- | [[Category: Specificity]]
| + | |
- | [[Category: Toxin]]
| + | |
| Structural highlights
Function
Q47644_ECOLX
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
BACKGROUND: Shiga-like toxins (SLTs) are produced by the pathogenic strains of Escherichia coli that cause hemorrhagic colitis and hemolytic uremic syndrome. These diseases in humans are generally associated with group II family members (SLT-II and SLT-IIc), whereas SLT-IIe (pig edema toxin) is central to edema disease of swine. The pentameric B-subunit component of the majority of family members binds to the cell-surface glycolipid globotriaosyl ceramide (Gb(3)), but globotetraosyl ceramide (Gb(4)) is the preferred receptor for SLT-IIe. A double-mutant of the SLT-IIe B subunit that reverses two sequence differences from SLT-II (GT3; Gln65-->Glu, Lys67-->Gln, SLT-I numbering) has been shown to bind more strongly to Gb(3) than to Gb(4). RESULTS: To understand the molecular basis of receptor binding and specificity, we have determined the structure of the GT3 mutant B pentamer, both in complex with a Gb(3) analogue (2.0 A resolution; R = 0.155, R(free) = 0.194) and in its native form (2.35 A resolution; R = 0.187, R(free) = 0.232). CONCLUSIONS: These are the first structures of a member of the medically important group II Shiga-like toxins to be reported. The structures confirm the previous observation of multiple binding sites on each SLT monomer, although binding site 3 is not occupied in the GT3 structure. Analysis of the binding properties of mutants suggests that site 3 is a secondary Gb(4)-binding site. The two mutated residues are located appropriately to interact with the extra betaGalNAc residue on Gb(4). Differences in the binding sites provide a molecular basis for understanding the tissue specificities and pathogenic mechanisms of members of the SLT family.
A mutant Shiga-like toxin IIe bound to its receptor Gb(3): structure of a group II Shiga-like toxin with altered binding specificity.,Ling H, Pannu NS, Boodhoo A, Armstrong GD, Clark CG, Brunton JL, Read RJ Structure. 2000 Mar 15;8(3):253-64. PMID:10745005[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ling H, Pannu NS, Boodhoo A, Armstrong GD, Clark CG, Brunton JL, Read RJ. A mutant Shiga-like toxin IIe bound to its receptor Gb(3): structure of a group II Shiga-like toxin with altered binding specificity. Structure. 2000 Mar 15;8(3):253-64. PMID:10745005
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