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| | ==Structure of a bacterial self-associating protein== | | ==Structure of a bacterial self-associating protein== |
| - | <StructureSection load='4kh3' size='340' side='right' caption='[[4kh3]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='4kh3' size='340' side='right'caption='[[4kh3]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4kh3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecol6 Ecol6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KH3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KH3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4kh3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_CFT073 Escherichia coli CFT073]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KH3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KH3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</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]] 2.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dab|1dab]], [[3h09|3h09]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">agn43, c3655 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=199310 ECOL6])</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=4kh3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kh3 OCA], [https://pdbe.org/4kh3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kh3 RCSB], [https://www.ebi.ac.uk/pdbsum/4kh3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kh3 ProSAT]</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=4kh3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kh3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kh3 RCSB], [http://www.ebi.ac.uk/pdbsum/4kh3 PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/A0A0H2VAW5_ECOL6 A0A0H2VAW5_ECOL6] |
| - | Aggregation and biofilm formation are critical mechanisms for bacterial resistance to host immune factors and antibiotics. Autotransporter (AT) proteins, which represent the largest group of outer-membrane and secreted proteins in Gram-negative bacteria, contribute significantly to these phenotypes. Despite their abundance and role in bacterial pathogenesis, most AT proteins have not been structurally characterized, and there is a paucity of detailed information with regard to their mode of action. Here we report the structure-function relationships of Antigen 43 (Ag43a), a prototypic self-associating AT protein from uropathogenic Escherichia coli. The functional domain of Ag43a displays a twisted L-shaped beta-helical structure firmly stabilized by a 3D hydrogen-bonded scaffold. Notably, the distinctive Ag43a L shape facilitates self-association and cell aggregation. Combining all our data, we define a molecular "Velcro-like" mechanism of AT-mediated bacterial clumping, which can be tailored to fit different bacterial lifestyles such as the formation of biofilms.
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| - | The antigen 43 structure reveals a molecular Velcro-like mechanism of autotransporter-mediated bacterial clumping.,Heras B, Totsika M, Peters KM, Paxman JJ, Gee CL, Jarrott RJ, Perugini MA, Whitten AE, Schembri MA Proc Natl Acad Sci U S A. 2014 Jan 7;111(1):457-62. doi: 10.1073/pnas.1311592111., Epub 2013 Dec 13. PMID:24335802<ref>PMID:24335802</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecol6]] | + | [[Category: Escherichia coli CFT073]] |
| - | [[Category: Gee, C L]] | + | [[Category: Large Structures]] |
| - | [[Category: Heras, B]] | + | [[Category: Gee CL]] |
| - | [[Category: Schembri, M A]] | + | [[Category: Heras B]] |
| - | [[Category: Totsika, M]] | + | [[Category: Schembri MA]] |
| - | [[Category: Ag43]] | + | [[Category: Totsika M]] |
| - | [[Category: Aggregation]]
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| - | [[Category: Aida-i type autotransporter]]
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| - | [[Category: Biofilm]]
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| - | [[Category: Immune system]]
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| - | [[Category: Self-associating protein]]
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| - | [[Category: Uropathogenic escherichia coli]]
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