5d6h: Difference between revisions

(2 intermediate revisions by the same user not shown)

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 5d6h is ~~ON HOLD until Paper~~ Publication

==Crystal structure of CsuC-CsuA/B chaperone-major subunit pre-assembly complex from Csu biofilm-mediating pili of Acinetobacter baumannii==

== Structural highlights ==

<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='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>

</table>

== Function ==

[https://www.uniprot.org/uniprot/Q6XBY4_ACIBA Q6XBY4_ACIBA]

== 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.

~~Authors:~~ Pakharukova, N~~.A.~~, ~~Tuitilla~~, M., Paavilainen, S., Zavialov, A.

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>

~~Description: Crystal structure~~ of ~~CsuC-CsuA~~/~~B chaperone~~-~~major subunit pre~~-~~assembly complex from Csu biofilm-mediating pili of~~ Acinetobacter baumannii

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

[[Category: ~~Tuitilla, M~~]]

[[Category: ~~Zavialov, A~~]]

== References ==

[[Category: ~~Paavilainen, S~~]]

[[Category: ~~Pakharukova, N.~~A]]

__TOC__

</StructureSection>

[[Category: Acinetobacter baumannii]]

[[Category: Large Structures]]

[[Category: Paavilainen S]]

[[Category: Pakharukova NA]]

[[Category: Tuitilla M]]

[[Category: Zavialov A]]

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5d6h is ON HOLD  until Paper Publication
+==Crystal structure of CsuC-CsuA/B chaperone-major subunit pre-assembly complex from Csu biofilm-mediating pili of Acinetobacter baumannii==
+<StructureSection load='5d6h' size='340' side='right'caption='[[5d6h]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+== Structural highlights ==
+<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='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>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q6XBY4_ACIBA Q6XBY4_ACIBA]
+<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.
-Authors: Pakharukova, N.A., Tuitilla, M., Paavilainen, S., Zavialov, A.
+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>
-Description: Crystal structure of CsuC-CsuA/B chaperone-major subunit pre-assembly complex from Csu biofilm-mediating pili of Acinetobacter baumannii
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Tuitilla, M]]
+<div class="pdbe-citations 5d6h" style="background-color:#fffaf0;"></div>
-[[Category: Zavialov, A]]
+== References ==
-[[Category: Paavilainen, S]]
+<references/>
-[[Category: Pakharukova, N.A]]
+__TOC__
+</StructureSection>
+[[Category: Acinetobacter baumannii]]
+[[Category: Large Structures]]
+[[Category: Paavilainen S]]
+[[Category: Pakharukova NA]]
+[[Category: Tuitilla M]]
+[[Category: Zavialov A]]