5d6h: Difference between revisions
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<StructureSection load='5d6h' size='340' side='right'caption='[[5d6h]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='5d6h' size='340' side='right'caption='[[5d6h]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5d6h]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5d6h]] is a 2 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=5D6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D6H FirstGlance]. <br> | ||
</td></tr><tr id=' | </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=5d6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d6h OCA], [https://pdbe.org/5d6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d6h RCSB], [https://www.ebi.ac.uk/pdbsum/5d6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d6h ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q6XBY4_ACIBA Q6XBY4_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: | [[Category: Acinetobacter baumannii]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Paavilainen | [[Category: Paavilainen S]] | ||
[[Category: Pakharukova | [[Category: Pakharukova NA]] | ||
[[Category: Tuitilla | [[Category: Tuitilla M]] | ||
[[Category: Zavialov | [[Category: Zavialov A]] | ||
Latest revision as of 13:23, 21 June 2023
Crystal structure of CsuC-CsuA/B chaperone-major subunit pre-assembly complex from Csu biofilm-mediating pili of Acinetobacter baumanniiCrystal structure of CsuC-CsuA/B chaperone-major subunit pre-assembly complex from Csu biofilm-mediating pili of Acinetobacter baumannii
Structural highlights
FunctionPublication Abstract from PubMedGram-negative pathogens express fibrous adhesive organelles that mediate targeting to sites of infection. The major class of these organelles is assembled via the classical, alternative and archaic chaperone-usher pathways. Although non-classical systems share a wider phylogenetic distribution and are associated with a range of diseases, little is known about their assembly mechanisms. Here we report atomic-resolution insight into the structure and biogenesis of Acinetobacter baumannii Csu and Escherichia coli ECP biofilm-mediating pili. We show that the two non-classical systems are structurally related, but their assembly mechanism is strikingly different from the classical assembly pathway. Non-classical chaperones, unlike their classical counterparts, maintain subunits in a substantially disordered conformational state, akin to a molten globule. This is achieved by a unique binding mechanism involving the register-shifted donor strand complementation and a different subunit carboxylate anchor. The subunit lacks the classical pre-folded initiation site for donor strand exchange, suggesting that recognition of its exposed hydrophobic core starts the assembly process and provides fresh inspiration for the design of inhibitors targeting chaperone-usher systems. Structural Insight into Archaic and Alternative Chaperone-Usher Pathways Reveals a Novel Mechanism of Pilus Biogenesis.,Pakharukova N, Garnett JA, Tuittila M, Paavilainen S, Diallo M, Xu Y, Matthews SJ, Zavialov AV PLoS Pathog. 2015 Nov 20;11(11):e1005269. doi: 10.1371/journal.ppat.1005269., eCollection 2015 Nov. PMID:26587649[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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