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| | ==Crystal structure of self-complemented CsuA/B major subunit from archaic chaperone-usher Csu pili of Acinetobacter baumannii== | | ==Crystal structure of self-complemented CsuA/B major subunit from archaic chaperone-usher Csu pili of Acinetobacter baumannii== |
| - | <StructureSection load='6fm5' size='340' side='right' caption='[[6fm5]], [[Resolution|resolution]] 1.47Å' scene=''> | + | <StructureSection load='6fm5' size='340' side='right'caption='[[6fm5]], [[Resolution|resolution]] 1.47Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6fm5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aciba Aciba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FM5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FM5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6fm5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FM5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FM5 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">csuA/B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=470 ACIBA])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.47Å</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=6fm5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fm5 OCA], [http://pdbe.org/6fm5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fm5 RCSB], [http://www.ebi.ac.uk/pdbsum/6fm5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fm5 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=6fm5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fm5 OCA], [https://pdbe.org/6fm5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fm5 RCSB], [https://www.ebi.ac.uk/pdbsum/6fm5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fm5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q6XBY7_ACIBA Q6XBY7_ACIBA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aciba]] | + | [[Category: Acinetobacter baumannii]] |
| - | [[Category: Paavilainen, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Pakharukova, N A]] | + | [[Category: Paavilainen S]] |
| - | [[Category: Tuitilla, M]] | + | [[Category: Pakharukova NA]] |
| - | [[Category: Zavialov, A V]] | + | [[Category: Tuitilla M]] |
| - | [[Category: Beta sandwich]] | + | [[Category: Zavialov AV]] |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Donor-strand complementation]]
| + | |
| - | [[Category: Ig-like fold]]
| + | |
| Structural highlights
Function
Q6XBY7_ACIBA
Publication Abstract from PubMed
Adhesive pili are external component of fibrous adhesive organelles and help bacteria attach to biotic or abiotic surfaces. The biogenesis of adhesive pili via the chaperone-usher pathway (CUP) is independent of external energy sources. In the classical CUP, chaperones transport assembly-competent pilins in a folded but expanded conformation. During donor-strand exchange, pilins subsequently collapse, producing a tightly-packed hydrophobic core and releasing the necessary free energy to drive fiber formation. Here, we show that pilus biogenesis in non-classical, archaic, and alternative CUPs uses a different source of conformational energy. High-resolution structures of the archaic Csu-pili system from Acinetobacter baumannii revealed that non-classical chaperones employ a short donor-strand motif that is insufficient to fully complement the pilin fold. This results in chaperone-bound pilins being trapped in a substantially unfolded intermediate. The exchange of this short motif with the longer donor strand from adjacent pilin provides the full steric information essential for folding, and thereby induces a large unfolded-to-folded conformational transition to drive assembly. Our findings may inform the development of anti-adhesion drugs (pilicides) to combat bacterial infections.
Archaic and alternative chaperones preserve pilin folding energy by providing incomplete structural information.,Pakharukova N, McKenna S, Tuittila M, Paavilainen S, Malmi H, Xu Y, Parilova O, Matthews S, Zavialov AV J Biol Chem. 2018 Sep 18. pii: RA118.004170. doi: 10.1074/jbc.RA118.004170. PMID:30228191[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pakharukova N, McKenna S, Tuittila M, Paavilainen S, Malmi H, Xu Y, Parilova O, Matthews S, Zavialov AV. Archaic and alternative chaperones preserve pilin folding energy by providing incomplete structural information. J Biol Chem. 2018 Sep 18. pii: RA118.004170. doi: 10.1074/jbc.RA118.004170. PMID:30228191 doi:http://dx.doi.org/10.1074/jbc.RA118.004170
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