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[[Image:2co4.gif|left|200px]]
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{{STRUCTURE_2co4|  PDB=2co4  |  SCENE=  }}
'''SALMONELLA ENTERICA SAFA PILIN IN COMPLEX WITH A 19-RESIDUE SAFA NTE PEPTIDE'''


==Salmonella enterica SafA pilin in complex with a 19-residue SafA Nte peptide==
<StructureSection load='2co4' size='340' side='right'caption='[[2co4]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</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>
== Function ==
[https://www.uniprot.org/uniprot/Q8ZRK4_SALTY Q8ZRK4_SALTY]
<div style="background-color:#fffaf0;">
== 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.


==Overview==
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<ref>PMID:16793551</ref>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2CO4 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CO4 OCA].
</div>
<div class="pdbe-citations 2co4" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/16793551 16793551]
*[[Pilin 3D structures|Pilin 3D structures]]
[[Category: Protein complex]]
== References ==
[[Category: Salmonella typhimurium]]
<references/>
[[Category: Ashcroft, A E.]]
__TOC__
[[Category: Hannan, T J.]]
</StructureSection>
[[Category: Hultgren, S J.]]
[[Category: Large Structures]]
[[Category: Radford, S E.]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: Remaut, H.]]
[[Category: Ashcroft AE]]
[[Category: Rose, R J.]]
[[Category: Hannan TJ]]
[[Category: Waksman, G.]]
[[Category: Hultgren SJ]]
[[Category: Fibril protein]]
[[Category: Radford SE]]
[[Category: Fold complementation]]
[[Category: Remaut H]]
[[Category: Pilus subunit adhesion pathogenesis]]
[[Category: Rose RJ]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 22:38:27 2008''
[[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

2co4 is a 2 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.85Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8ZRK4_SALTY

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.

See Also

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

2co4, resolution 1.85Å

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