View source for 7kob


==Crystal structure of antigen 43b from Escherichia coli CFT073==
<StructureSection load='7kob' size='340' side='right'caption='[[7kob]], [[Resolution|resolution]] 2.08&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7kob]] 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=7KOB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KOB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.08&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=7kob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kob OCA], [https://pdbe.org/7kob PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kob RCSB], [https://www.ebi.ac.uk/pdbsum/7kob PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kob ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0H2V731_ECOL6 A0A0H2V731_ECOL6] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The formation of aggregates and biofilms enhances bacterial colonisation and infection progression by affording protection from antibiotics and host immune factors. Despite these advantages there is a trade-off, whereby bacterial dissemination is reduced. As such, biofilm development needs to be controlled to suit adaptation to different environments. Here we investigate members from one of largest groups of bacterial adhesins, the autotransporters, for their critical role in the assembly of bacterial aggregates and biofilms. We describe the structural and functional characterisation of autotransporter Ag43 variants from different Escherichia coli pathotypes. We show that specific interactions between amino acids on the contacting interfaces of adjacent Ag43 proteins drives a common mode of trans-association that leads to cell clumping. Furthermore, subtle variation of these interactions alters aggregation kinetics and the degree of compacting within cell clusters. Together, our structure-function investigation reveals an underlying molecular basis for variations in the density of bacterial communities.

Variation of Antigen 43 self-association modulates bacterial compacting within aggregates and biofilms.,Vo JL, Ortiz GCM, Totsika M, Lo AW, Hancock SJ, Whitten AE, Hor L, Peters KM, Ageorges V, Caccia N, Desvaux M, Schembri MA, Paxman JJ, Heras B NPJ Biofilms Microbiomes. 2022 Apr 8;8(1):20. doi: 10.1038/s41522-022-00284-1. PMID:35396507<ref>PMID:35396507</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7kob" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli CFT073]]
[[Category: Large Structures]]
[[Category: Heras B]]
[[Category: Hor L]]
[[Category: Martinez-Ortiz GC]]
[[Category: Paxman JJ]]