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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/Q8ZRK4_SALTY Q8ZRK4_SALTY] | | [https://www.uniprot.org/uniprot/Q8ZRK4_SALTY Q8ZRK4_SALTY] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| 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.
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| 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>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 2co2" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Pilin 3D structures|Pilin 3D structures]] | | *[[Pilin 3D structures|Pilin 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |