5d55: Difference between revisions
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New page: '''Unreleased structure''' The entry 5d55 is ON HOLD Authors: Lee, W-C., Garnett, J.A., Matthews, S.J. Description: Category: Unreleased Structures Category: Matthews, S.J [[C... |
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==Crystal structure of the E. coli Hda pilus minor tip subunit, HdaB== | |||
<StructureSection load='5d55' size='340' side='right'caption='[[5d55]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5d55]] is a 2 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=5D55 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D55 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]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</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=5d55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d55 OCA], [https://pdbe.org/5d55 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d55 RCSB], [https://www.ebi.ac.uk/pdbsum/5d55 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d55 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/B3V224_ECOLX B3V224_ECOLX] [https://www.uniprot.org/uniprot/Q08JP6_ECOLX Q08JP6_ECOLX] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Enteroaggregative Escherichia coli is the primary cause of pediatric diarrhea in developing countries. They utilize aggregative adherence fimbriae (AAFs) to promote initial adherence to the host intestinal mucosa, promote the formation of biofilms, and mediate host invasion. Five AAFs have been identified to date and AAF/IV is amongst the most prevalent found in clinical isolates. Here we present the X-ray crystal structure of the AAF/IV tip protein HdaB at 2.0 A resolution. It shares high structural homology with members of the Afa/Dr superfamily of fimbriae, which are involved in host invasion. We highlight surface exposed residues that share sequence homology and propose that these may function in invasion and also non-conserved regions that could mediate HdaB specific adhesive functions. | |||
Crystal structure and analysis of HdaB: The enteroaggregative Escherichia coli AAF/IV pilus tip protein.,Lee WC, Matthews S, Garnett JA Protein Sci. 2016 Jul 12. doi: 10.1002/pro.2982. PMID:27400770<ref>PMID:27400770</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5d55" style="background-color:#fffaf0;"></div> | ||
[[Category: Garnett | == References == | ||
[[Category: Lee | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | |||
[[Category: Garnett JA]] | |||
[[Category: Lee W-C]] | |||
[[Category: Matthews SJ]] | |||
Latest revision as of 11:24, 10 January 2024
Crystal structure of the E. coli Hda pilus minor tip subunit, HdaB
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