5dfk: Difference between revisions
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''' | ==Crystal Structure of the Escherichia coli Common Pilus Chaperone, EcpB== | ||
<StructureSection load='5dfk' size='340' side='right' caption='[[5dfk]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5dfk]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DFK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DFK FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5d6h|5d6h]]</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=5dfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dfk OCA], [http://pdbe.org/5dfk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dfk RCSB], [http://www.ebi.ac.uk/pdbsum/5dfk PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/ECPB_ECO45 ECPB_ECO45]] Part of the ecpRABCDE operon, which encodes the E.coli common pilus (ECP). ECP is found in both commensal and pathogenic strains and plays a dual role in early-stage biofilm development and host cell recognition (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Gram-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<ref>PMID:26587649</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5dfk" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Diallo, M]] | [[Category: Diallo, M]] | ||
[[Category: Garnett, J. | [[Category: Garnett, J A]] | ||
[[Category: Matthews, S J]] | |||
[[Category: Adhesion]] | |||
[[Category: Biofilm]] | |||
[[Category: Biogenesis]] | |||
[[Category: Chaperone usher]] | |||
[[Category: E. coli]] | |||
[[Category: Pili]] | |||
[[Category: Pilus]] | |||
[[Category: Structural protein]] | |||
[[Category: Virulence]] | |||
