3x2r

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Current revision (08:48, 20 March 2024) (edit) (undo)
 
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<StructureSection load='3x2r' size='340' side='right'caption='[[3x2r]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='3x2r' size='340' side='right'caption='[[3x2r]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3x2r]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_xuzhou21 Escherichia coli xuzhou21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3X2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3X2R FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3x2r]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_Xuzhou21 Escherichia coli Xuzhou21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3X2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3X2R FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4q79|4q79]]</div></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]] 2.9&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CDCO157_1350, csgG ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=741093 Escherichia coli Xuzhou21])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3x2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3x2r OCA], [https://pdbe.org/3x2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3x2r RCSB], [https://www.ebi.ac.uk/pdbsum/3x2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3x2r 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=3x2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3x2r OCA], [https://pdbe.org/3x2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3x2r RCSB], [https://www.ebi.ac.uk/pdbsum/3x2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3x2r ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A0F6C2F5_ECOLX A0A0F6C2F5_ECOLX] May be involved in the biogenesis of curli organelles.[ARBA:ARBA00003989]
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Various strains of bacteria are able to produce a unique class of functional amyloids termed curli, which are critical for biofilm formation, host cell adhesion, and colonization of inert surfaces. Curli are secreted via the type VIII bacterial secretion system, and they share biochemical and structural characteristics with amyloid fibers that have been implicated in deleterious disease in humans. Here, we report the crystal structure of Escherichia coli CsgG, which is an essential lipoprotein component of the type VIII secretion system and which forms a secretion channel in the bacterial outer membrane for transporting curli subunits. CsgG forms a crown-shaped, symmetric nonameric channel that spans the outer membrane via a 36-strand beta-barrel, with each subunit contributing four beta-strands. This nonameric complex contains a central channel with a pore located at the middle. The eyelet of the pore is approximately 12 A in diameter and is lined with three stacked nine-residue rings consisting of Tyr-66, Asn-70, or Phe-71. Our structure-based functional studies suggest that Tyr-66 and Phe-71 residues function as gatekeepers for the selective secretion of curli subunits. Our study describes in detail, to our knowledge, the first core structure of the type VIII bacterial secretion machinery. Importantly, our structural analysis suggests that the curli subunits are secreted via CsgG across the bacterial outer membrane in an unfolded form.
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Structure of the nonameric bacterial amyloid secretion channel.,Cao B, Zhao Y, Kou Y, Ni D, Zhang XC, Huang Y Proc Natl Acad Sci U S A. 2014 Dec 1. pii: 201411942. PMID:25453093<ref>PMID:25453093</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 3x2r" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Escherichia coli xuzhou21]]
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[[Category: Escherichia coli Xuzhou21]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cao, B]]
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[[Category: Cao B]]
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[[Category: Huang, Y]]
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[[Category: Huang Y]]
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[[Category: Kou, Y]]
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[[Category: Kou Y]]
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[[Category: Ni, D]]
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[[Category: Ni D]]
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[[Category: Zhang, X C]]
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[[Category: Zhang XC]]
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[[Category: Zhao, Y]]
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[[Category: Zhao Y]]
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[[Category: Beta-barrel]]
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[[Category: Biofim]]
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[[Category: Curli secretion]]
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[[Category: Membrane protein]]
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[[Category: Outer membrane protein]]
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Current revision

Structure of the nonameric bacterial amyloid secretion channel CsgG

PDB ID 3x2r

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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