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3ml3

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Current revision (08:48, 7 February 2024) (edit) (undo)
 
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<StructureSection load='3ml3' size='340' side='right'caption='[[3ml3]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3ml3' size='340' side='right'caption='[[3ml3]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ml3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"shigella_paradysenteriae"_weldin_1927 "shigella paradysenteriae" weldin 1927]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ML3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ML3 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ml3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ML3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ML3 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CP0182, icsA, virG ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 "Shigella paradysenteriae" Weldin 1927])</td></tr>
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</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&#8491;</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=3ml3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ml3 OCA], [https://pdbe.org/3ml3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ml3 RCSB], [https://www.ebi.ac.uk/pdbsum/3ml3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ml3 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=3ml3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ml3 OCA], [https://pdbe.org/3ml3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ml3 RCSB], [https://www.ebi.ac.uk/pdbsum/3ml3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ml3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/ICSA_SHIFL ICSA_SHIFL]] Essential for bacterial spreading by eliciting polar deposition of filamentous actin (actin-based motility). Inside the host cell mediates nucleation and polymerization of actin molecules on the bacterial surface, which provides the propulsive force for intracellular movement and intercellular dissemination of the bacterium. During invasion of mammalian cells, triggers autophagy by binding to APG5L. Interaction with IcsB leads to escape from the autophagic host defense system. Also binds ATP and displays weak ATPase activity.<ref>PMID:7896693</ref> <ref>PMID:2542950</ref> <ref>PMID:1602963</ref> <ref>PMID:9582270</ref> <ref>PMID:15576571</ref>
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[https://www.uniprot.org/uniprot/ICSA_SHIFL ICSA_SHIFL] Essential for bacterial spreading by eliciting polar deposition of filamentous actin (actin-based motility). Inside the host cell mediates nucleation and polymerization of actin molecules on the bacterial surface, which provides the propulsive force for intracellular movement and intercellular dissemination of the bacterium. During invasion of mammalian cells, triggers autophagy by binding to APG5L. Interaction with IcsB leads to escape from the autophagic host defense system. Also binds ATP and displays weak ATPase activity.<ref>PMID:7896693</ref> <ref>PMID:2542950</ref> <ref>PMID:1602963</ref> <ref>PMID:9582270</ref> <ref>PMID:15576571</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The IcsA (intracellular spread gene A) autotransporter from Shigella flexneri is a key virulence factor. We identified a stable fragment comprising residues 591 to 758, which corresponds to the autochaperone region of the IcsA passenger domain. We showed that thermal unfolding of the autochaperone region is reversible and determined its crystal structure at 2.0-A resolution.
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Crystal Structure of the Autochaperone Region from the Shigella flexneri Autotransporter IcsA.,Kuhnel K, Diezmann D J Bacteriol. 2011 Apr;193(8):2042-5. Epub 2011 Feb 18. PMID:21335457<ref>PMID:21335457</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3ml3" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Shigella paradysenteriae weldin 1927]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Diezmann, D]]
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[[Category: Shigella flexneri]]
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[[Category: Kuhnel, K]]
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[[Category: Diezmann D]]
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[[Category: Beta helix]]
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[[Category: Kuhnel K]]
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[[Category: Beta sandwich]]
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[[Category: Protein transport]]
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Current revision

Crystal structure of the IcsA autochaperone region

PDB ID 3ml3

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