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| | <StructureSection load='2jkj' size='340' side='right'caption='[[2jkj]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='2jkj' size='340' side='right'caption='[[2jkj]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jkj]] is a 6 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=2JKJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JKJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jkj]] is a 6 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=2JKJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JKJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLM:CHLORAMPHENICOL'>CLM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TH8:THIAMPHENICOL'>TH8</scene></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]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1usq|1usq]], [[1ut1|1ut1]], [[2jkl|2jkl]], [[2jkn|2jkn]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLM:CHLORAMPHENICOL'>CLM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TH8:THIAMPHENICOL'>TH8</scene></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=2jkj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jkj OCA], [https://pdbe.org/2jkj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jkj RCSB], [https://www.ebi.ac.uk/pdbsum/2jkj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jkj 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=2jkj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jkj OCA], [https://pdbe.org/2jkj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jkj RCSB], [https://www.ebi.ac.uk/pdbsum/2jkj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jkj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/DRAA_ECOLX DRAA_ECOLX] Hemagglutinins of uropathogenic E.coli mediate adherence to the upper urinary tract. These adhesins bind to the Dr blood group antigen and also agglutinate human erythrocytes in the presence of D-mannose (mannose-resistant hemagglutination (MRHA)). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Davies, S G]] | + | [[Category: Davies SG]] |
| - | [[Category: Lea, S M]] | + | [[Category: Lea SM]] |
| - | [[Category: Pettigrew, D M]] | + | [[Category: Pettigrew DM]] |
| - | [[Category: Roversi, P]] | + | [[Category: Roversi P]] |
| - | [[Category: Russell, A J]] | + | [[Category: Russell AJ]] |
| - | [[Category: Adhesin]]
| + | |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Cell projection]]
| + | |
| - | [[Category: Chloramphenicol succinate]]
| + | |
| - | [[Category: Daec]]
| + | |
| - | [[Category: Drae]]
| + | |
| - | [[Category: Fimbrial adhesin]]
| + | |
| - | [[Category: Fimbrium]]
| + | |
| - | [[Category: Haemagglutinin]]
| + | |
| - | [[Category: Upec]]
| + | |
| Structural highlights
Function
DRAA_ECOLX Hemagglutinins of uropathogenic E.coli mediate adherence to the upper urinary tract. These adhesins bind to the Dr blood group antigen and also agglutinate human erythrocytes in the presence of D-mannose (mannose-resistant hemagglutination (MRHA)).
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
Dr adhesins are expressed on the surface of uropathogenic and diffusely adherent strains of Escherichia coli. The major adhesin subunit (DraE/AfaE) of these organelles mediates attachment of the bacterium to the surface of the host cell and possibly intracellular invasion through its recognition of the complement regulator decay-accelerating factor (DAF) and/or members of the carcinoembryonic antigen (CEA) family. The adhesin subunit of the Dr haemagglutinin, a Dr-family member, additionally binds type IV collagen and is inhibited in all its receptor interactions by the antibiotic chloramphenicol (CLM). In this study, previous structural work is built upon by reporting the X-ray structures of DraE bound to two chloramphenicol derivatives: chloramphenicol succinate (CLS) and bromamphenicol (BRM). The CLS structure demonstrates that acylation of the 3-hydroxyl group of CLM with succinyl does not significantly perturb the mode of binding, while the BRM structure implies that the binding pocket is able to accommodate bulkier substituents on the N-acyl group. It is concluded that modifications of the 3-hydroxyl group would generate a potent Dr haemagglutinin inhibitor that would not cause the toxic side effects that are associated with the normal bacteriostatic activity of CLM.
A structural study of the interaction between the Dr haemagglutinin DraE and derivatives of chloramphenicol.,Pettigrew DM, Roversi P, Davies SG, Russell AJ, Lea SM Acta Crystallogr D Biol Crystallogr. 2009 Jun;65(Pt 6):513-22. Epub 2009, May 15. PMID:19465765[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Pettigrew DM, Roversi P, Davies SG, Russell AJ, Lea SM. A structural study of the interaction between the Dr haemagglutinin DraE and derivatives of chloramphenicol. Acta Crystallogr D Biol Crystallogr. 2009 Jun;65(Pt 6):513-22. Epub 2009, May 15. PMID:19465765 doi:10.1107/S0907444909005113
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