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| | ==Crystal structure of the IcsA autochaperone region== | | ==Crystal structure of the IcsA autochaperone region== |
| - | <StructureSection load='3ml3' size='340' side='right' caption='[[3ml3]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='3ml3' size='340' side='right'caption='[[3ml3]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ml3]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ML3 FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CP0182, icsA, virG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 "Shigella paradysenteriae" Weldin 1927])</td></tr> | + | </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> |
| - | <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=3ml3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ml3 OCA], [http://pdbe.org/3ml3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ml3 RCSB], [http://www.ebi.ac.uk/pdbsum/3ml3 PDBsum], [http://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 == |
| - | [[http://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> | + | [[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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Shigella paradysenteriae weldin 1927]] | | [[Category: Shigella paradysenteriae weldin 1927]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Diezmann, D]] | | [[Category: Diezmann, D]] |
| | [[Category: Kuhnel, K]] | | [[Category: Kuhnel, K]] |
| Structural highlights
Function
[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.[1] [2] [3] [4] [5]
Publication Abstract from PubMed
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.
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[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fukuda I, Suzuki T, Munakata H, Hayashi N, Katayama E, Yoshikawa M, Sasakawa C. Cleavage of Shigella surface protein VirG occurs at a specific site, but the secretion is not essential for intracellular spreading. J Bacteriol. 1995 Apr;177(7):1719-26. PMID:7896693
- ↑ Bernardini ML, Mounier J, d'Hauteville H, Coquis-Rondon M, Sansonetti PJ. Identification of icsA, a plasmid locus of Shigella flexneri that governs bacterial intra- and intercellular spread through interaction with F-actin. Proc Natl Acad Sci U S A. 1989 May;86(10):3867-71. PMID:2542950
- ↑ d'Hauteville H, Sansonetti PJ. Phosphorylation of IcsA by cAMP-dependent protein kinase and its effect on intracellular spread of Shigella flexneri. Mol Microbiol. 1992 Apr;6(7):833-41. PMID:1602963
- ↑ Suzuki T, Miki H, Takenawa T, Sasakawa C. Neural Wiskott-Aldrich syndrome protein is implicated in the actin-based motility of Shigella flexneri. EMBO J. 1998 May 15;17(10):2767-76. PMID:9582270 doi:10.1093/emboj/17.10.2767
- ↑ Ogawa M, Yoshimori T, Suzuki T, Sagara H, Mizushima N, Sasakawa C. Escape of intracellular Shigella from autophagy. Science. 2005 Feb 4;307(5710):727-31. Epub 2004 Dec 2. PMID:15576571 doi:10.1126/science.1106036
- ↑ Kuhnel K, Diezmann D. Crystal Structure of the Autochaperone Region from the Shigella flexneri Autotransporter IcsA. J Bacteriol. 2011 Apr;193(8):2042-5. Epub 2011 Feb 18. PMID:21335457 doi:10.1128/JB.00790-10
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