View source for 4uv2


==Structure of the curli transport lipoprotein CsgG in a non-lipidated, pre-pore conformation==
<StructureSection load='4uv2' size='340' side='right'caption='[[4uv2]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4uv2]] is a 16 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=4UV2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UV2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4uv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uv2 OCA], [https://pdbe.org/4uv2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uv2 RCSB], [https://www.ebi.ac.uk/pdbsum/4uv2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uv2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CSGG_ECOLI CSGG_ECOLI] May be involved in the biogenesis of curli organelles.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Curli 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<ref>PMID:25219853</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4uv2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli str. K-12 substr. MC4100]]
[[Category: Large Structures]]
[[Category: Broeck IVD]]
[[Category: Chapman MR]]
[[Category: Fronzes R]]
[[Category: Gerven NV]]
[[Category: Goyal P]]
[[Category: Gubellini F]]
[[Category: Howorka S]]
[[Category: Hultgren SJ]]
[[Category: Jonckheere W]]
[[Category: Krasteva PV]]
[[Category: Pehau-Arnaudet G]]
[[Category: Pinkner JS]]
[[Category: Remaut H]]
[[Category: Troupiotis-Tsailaki A]]