4uv3: Difference between revisions
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==Structure of the curli transport lipoprotein CsgG in its membrane- bound conformation== | ==Structure of the curli transport lipoprotein CsgG in its membrane- bound conformation== | ||
<StructureSection load='4uv3' size='340' side='right' caption='[[4uv3]], [[Resolution|resolution]] 3.59Å' scene=''> | <StructureSection load='4uv3' size='340' side='right'caption='[[4uv3]], [[Resolution|resolution]] 3.59Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4uv3]] is a 18 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UV3 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4uv3]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._MC4100 Escherichia coli str. K-12 substr. MC4100]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UV3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UV3 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.59Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4uv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uv3 OCA], [https://pdbe.org/4uv3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uv3 RCSB], [https://www.ebi.ac.uk/pdbsum/4uv3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uv3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/CSGG_ECOLI CSGG_ECOLI] May be involved in the biogenesis of curli organelles. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 16: | Line 17: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4uv3" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Broeck | [[Category: Escherichia coli str. K-12 substr. MC4100]] | ||
[[Category: Chapman | [[Category: Large Structures]] | ||
[[Category: Fronzes | [[Category: Broeck IVD]] | ||
[[Category: Gerven | [[Category: Chapman MR]] | ||
[[Category: Goyal | [[Category: Fronzes R]] | ||
[[Category: Gubellini | [[Category: Gerven NV]] | ||
[[Category: Howorka | [[Category: Goyal P]] | ||
[[Category: Hultgren | [[Category: Gubellini F]] | ||
[[Category: Jonckheere | [[Category: Howorka S]] | ||
[[Category: Krasteva | [[Category: Hultgren SJ]] | ||
[[Category: Pehau-Arnaudet | [[Category: Jonckheere W]] | ||
[[Category: Pinkner | [[Category: Krasteva PV]] | ||
[[Category: Remaut | [[Category: Pehau-Arnaudet G]] | ||
[[Category: Troupiotis-Tsailaki | [[Category: Pinkner JS]] | ||
[[Category: Remaut H]] | |||
[[Category: Troupiotis-Tsailaki A]] | |||
Latest revision as of 13:36, 10 January 2024
Structure of the curli transport lipoprotein CsgG in its membrane- bound conformationStructure of the curli transport lipoprotein CsgG in its membrane- bound conformation
Structural highlights
FunctionCSGG_ECOLI May be involved in the biogenesis of curli organelles. Publication Abstract from PubMedCurli are functional amyloid fibres that constitute the major protein component of the extracellular matrix in pellicle biofilms formed by Bacteroidetes and Proteobacteria (predominantly of the alpha and gamma classes). They provide a fitness advantage in pathogenic strains and induce a strong pro-inflammatory response during bacteraemia. Curli formation requires a dedicated protein secretion machinery comprising the outer membrane lipoprotein CsgG and two soluble accessory proteins, CsgE and CsgF. Here we report the X-ray structure of Escherichia coli CsgG in a non-lipidated, soluble form as well as in its native membrane-extracted conformation. CsgG forms an oligomeric transport complex composed of nine anticodon-binding-domain-like units that give rise to a 36-stranded beta-barrel that traverses the bilayer and is connected to a cage-like vestibule in the periplasm. The transmembrane and periplasmic domains are separated by a 0.9-nm channel constriction composed of three stacked concentric phenylalanine, asparagine and tyrosine rings that may guide the extended polypeptide substrate through the secretion pore. The specificity factor CsgE forms a nonameric adaptor that binds and closes off the periplasmic face of the secretion channel, creating a 24,000 A3 pre-constriction chamber. Our structural, functional and electrophysiological analyses imply that CsgG is an ungated, non-selective protein secretion channel that is expected to employ a diffusion-based, entropy-driven transport mechanism. Structural and mechanistic insights into the bacterial amyloid secretion channel CsgG.,Goyal P, Krasteva PV, Van Gerven N, Gubellini F, Van den Broeck I, Troupiotis-Tsailaki A, Jonckheere W, Pehau-Arnaudet G, Pinkner JS, Chapman MR, Hultgren SJ, Howorka S, Fronzes R, Remaut H Nature. 2014 Sep 14. doi: 10.1038/nature13768. PMID:25219853[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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