2co4: Difference between revisions
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<StructureSection load='2co4' size='340' side='right'caption='[[2co4]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='2co4' size='340' side='right'caption='[[2co4]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2co4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CO4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CO4 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2co4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CO4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CO4 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</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=2co4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2co4 OCA], [https://pdbe.org/2co4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2co4 RCSB], [https://www.ebi.ac.uk/pdbsum/2co4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2co4 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=2co4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2co4 OCA], [https://pdbe.org/2co4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2co4 RCSB], [https://www.ebi.ac.uk/pdbsum/2co4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2co4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8ZRK4_SALTY Q8ZRK4_SALTY] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 2co4" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2co4" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Pilin 3D structures|Pilin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ashcroft | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium]] | ||
[[Category: Hannan | [[Category: Ashcroft AE]] | ||
[[Category: Hultgren | [[Category: Hannan TJ]] | ||
[[Category: Radford | [[Category: Hultgren SJ]] | ||
[[Category: Remaut | [[Category: Radford SE]] | ||
[[Category: Rose | [[Category: Remaut H]] | ||
[[Category: Waksman | [[Category: Rose RJ]] | ||
[[Category: Waksman G]] | |||
Latest revision as of 13:26, 6 September 2023
Salmonella enterica SafA pilin in complex with a 19-residue SafA Nte peptideSalmonella enterica SafA pilin in complex with a 19-residue SafA Nte peptide
Structural highlights
FunctionPublication Abstract from PubMedGram-negative pathogens commonly use the chaperone-usher pathway to assemble adhesive multisubunit fibers on their surface. In the periplasm, subunits are stabilized by a chaperone that donates a beta strand to complement the subunits' truncated immunoglobulin-like fold. Pilus assembly proceeds through a "donor-strand exchange" (DSE) mechanism whereby this complementary beta strand is replaced by the N-terminal extension (Nte) of an incoming pilus subunit. Using X-ray crystallography and real-time electrospray ionization mass spectrometry (ESI-MS), we demonstrate that DSE requires the formation of a transient ternary complex between the chaperone-subunit complex and the Nte of the next subunit to be assembled. The process is crucially dependent on an initiation site (the P5 pocket) needed to recruit the incoming Nte. The data also suggest a capping reaction displacing DSE toward product formation. These results support a zip-in-zip-out mechanism for DSE and a catalytic role for the usher, the molecular platform at which pili are assembled. Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted beta strand displacement mechanism.,Remaut H, Rose RJ, Hannan TJ, Hultgren SJ, Radford SE, Ashcroft AE, Waksman G Mol Cell. 2006 Jun 23;22(6):831-42. PMID:16793551[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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