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4mee

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Revision as of 11:11, 21 December 2022

Crystal 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.
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]

Publication Abstract from PubMed

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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
↑ Gawarzewski I, DiMaio F, Winterer E, Tschapek B, Smits SH, Jose J, Schmitt L. Crystal structure of the transport unit of the autotransporter adhesin involved in diffuse adherence from Escherichia coli. J Struct Biol. 2014 May 16. pii: S1047-8477(14)00109-9. doi:, 10.1016/j.jsb.2014.05.003. PMID:24841284 doi:http://dx.doi.org/10.1016/j.jsb.2014.05.003

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='4mee' size='340' side='right'caption='[[4mee]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == 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='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>
-<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>
 </table>
+== Function ==
+[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 24: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[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]]

4mee

From Proteopedia

Revision as of 11:11, 21 December 2022

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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