4mee: Difference between revisions

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<StructureSection load='4mee' size='340' side='right'caption='[[4mee]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='4mee' size='340' side='right'caption='[[4mee]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4mee]] is a 1 chain structure with sequence from [http://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=4MEE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MEE FirstGlance]. <br>
<table><tr><td colspan='2'>[[4mee]] is a 1 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=4MEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MEE FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aidA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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]] 3&#8491;</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=4mee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mee OCA], [http://pdbe.org/4mee PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mee RCSB], [http://www.ebi.ac.uk/pdbsum/4mee PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mee 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=4mee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mee OCA], [https://pdbe.org/4mee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mee RCSB], [https://www.ebi.ac.uk/pdbsum/4mee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mee ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/AIDA_ECOLX AIDA_ECOLX] Potent bacterial adhesin that mediates bacterial attachment to a broad variety of human and other mammalian cells. AIDA possesses additional virulence properties, as it is capable of mediating bacterial autoaggregation via intercellular self-recognition and it is a highly efficient initiator of biofilm formation.<ref>PMID:15547278</ref>  
Several serious gastrointestinal diseases, which are widespread all over the world, are caused by enteropathogenic Escherichia coli. The monomeric autotransporter AIDA-I (adhesin involved in diffuse adherence) represents an important virulence factor of these strains and is involved in adhesion, biofilm formation, aggregation and invasion into host cells. Here, we present the crystal structure of the transport unit of AIDA-I at 3.0A resolution, which forms a 12-stranded beta-barrel harboring the linker domain in its pore. Mutagenesis studies of the C-terminal amino acid demonstrated the great impact of this terminal residue on membrane integration of AIDA-I and passenger translocation.
 
Crystal structure of the transport unit of the autotransporter adhesin involved in diffuse adherence from Escherichia coli.,Gawarzewski I, DiMaio F, Winterer E, Tschapek B, Smits SH, Jose J, Schmitt L J Struct Biol. 2014 May 16. pii: S1047-8477(14)00109-9. doi:, 10.1016/j.jsb.2014.05.003. PMID:24841284<ref>PMID:24841284</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4mee" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Gawarzewski, I]]
[[Category: Gawarzewski I]]
[[Category: Hoeppner, A]]
[[Category: Hoeppner A]]
[[Category: Jose, J]]
[[Category: Jose J]]
[[Category: Schmitt, L]]
[[Category: Schmitt L]]
[[Category: Smits, S H]]
[[Category: Smits SH]]
[[Category: Tschapek, B]]
[[Category: Tschapek B]]
[[Category: Autotransporter]]
[[Category: Beta barrel]]
[[Category: Outer membrane protein]]
[[Category: Protein binding]]

Latest revision as of 15:26, 1 March 2024

Crystal structure of the transport unit of the autotransporter AIDA-I from Escherichia coliCrystal structure of the transport unit of the autotransporter AIDA-I from Escherichia coli

Structural highlights

4mee is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AIDA_ECOLX Potent bacterial adhesin that mediates bacterial attachment to a broad variety of human and other mammalian cells. AIDA possesses additional virulence properties, as it is capable of mediating bacterial autoaggregation via intercellular self-recognition and it is a highly efficient initiator of biofilm formation.[1]

See Also

References

  1. ↑ Sherlock O, Schembri MA, Reisner A, Klemm P. Novel roles for the AIDA adhesin from diarrheagenic Escherichia coli: cell aggregation and biofilm formation. J Bacteriol. 2004 Dec;186(23):8058-65. PMID:15547278 doi:http://dx.doi.org/186/23/8058

4mee, resolution 3.00Å

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