2co3: Difference between revisions

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<StructureSection load='2co3' size='340' side='right'caption='[[2co3]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
<StructureSection load='2co3' size='340' side='right'caption='[[2co3]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2co3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Salty Salty]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CO3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CO3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2co3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salty Salty]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CO3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CO3 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2cny|2cny]], [[2cnz|2cnz]], [[2co1|2co1]], [[2co2|2co2]], [[2co4|2co4]], [[2co6|2co6]], [[2co7|2co7]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2cny|2cny]], [[2cnz|2cnz]], [[2co1|2co1]], [[2co2|2co2]], [[2co4|2co4]], [[2co6|2co6]], [[2co7|2co7]]</div></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=2co3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2co3 OCA], [http://pdbe.org/2co3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2co3 RCSB], [http://www.ebi.ac.uk/pdbsum/2co3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2co3 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=2co3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2co3 OCA], [https://pdbe.org/2co3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2co3 RCSB], [https://www.ebi.ac.uk/pdbsum/2co3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2co3 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">

Revision as of 23:36, 20 October 2021

Salmonella enterica SafA pilin, head-to-tail swapped dimer of Ntd1 mutantSalmonella enterica SafA pilin, head-to-tail swapped dimer of Ntd1 mutant

Structural highlights

2co3 is a 2 chain structure with sequence from Salty. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Gram-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.

References

  1. Remaut H, Rose RJ, Hannan TJ, Hultgren SJ, Radford SE, Ashcroft AE, Waksman G. Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted beta strand displacement mechanism. Mol Cell. 2006 Jun 23;22(6):831-42. PMID:16793551 doi:10.1016/j.molcel.2006.05.033

2co3, resolution 1.78Å

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