View source for 8odn


==RcpA-TadD with C13 symmetry from the Pseudomonas aeruginosa Tight Adherence Secretion System==
<StructureSection load='8odn' size='340' side='right'caption='[[8odn]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8odn]] is a 26 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ODN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ODN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.7&#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=8odn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8odn OCA], [https://pdbe.org/8odn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8odn RCSB], [https://www.ebi.ac.uk/pdbsum/8odn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8odn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9HW96_PSEAE Q9HW96_PSEAE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The bacterial Tight adherence Secretion System (TadSS) assembles surface pili that drive cell adherence, biofilm formation and bacterial predation. The structure and mechanism of the TadSS is mostly unknown. This includes characterisation of the outer membrane secretin through which the pilus is channelled and recruitment of its pilotin. Here we investigate RcpA and TadD lipoprotein from Pseudomonas aeruginosa. Light microscopy reveals RcpA colocalising with TadD in P. aeruginosa and when heterologously expressed in Escherichia coli. We use cryogenic electron microscopy to determine how RcpA and TadD assemble a secretin channel with C13 and C14 symmetries. Despite low sequence homology, we show that TadD shares a similar fold to the type 4 pilus system pilotin PilF. We establish that the C-terminal four residues of RcpA bind TadD - an interaction essential for secretin formation. The binding mechanism between RcpA and TadD appears distinct from known secretin-pilotin pairings in other secretion systems.

Assembly mechanism of a Tad secretion system secretin-pilotin complex.,Tassinari M, Rudzite M, Filloux A, Low HH Nat Commun. 2023 Sep 13;14(1):5643. doi: 10.1038/s41467-023-41200-1. PMID:37704603<ref>PMID:37704603</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8odn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa PAO1]]
[[Category: Low HH]]
[[Category: Tassinari M]]