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4kh3

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Structure of a bacterial self-associating protein

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Retrieved from "http://52.214.119.220/wiki/index.php/4kh3"

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 ==Structure of a bacterial self-associating protein==
-<StructureSection load='4kh3' size='340' side='right' caption='[[4kh3]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+<StructureSection load='4kh3' size='340' side='right'caption='[[4kh3]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == 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]] 2.5&#8491;</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://pdbe.org/4kh3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kh3 RCSB], [http://www.ebi.ac.uk/pdbsum/4kh3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kh3 ProSAT]</span></td></tr>
 </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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4kh3" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </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]]
-[[Category: Aida-i type autotransporter]]
-[[Category: Biofilm]]
-[[Category: Immune system]]
-[[Category: Self-associating protein]]
-[[Category: Uropathogenic escherichia coli]]

4kh3

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Structure of a bacterial self-associating protein

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