View source for 8wb8


==Crystal Structure of the shaft pilin LrpA from Ligilactobacillus ruminis - orthorhombic form==
<StructureSection load='8wb8' size='340' side='right'caption='[[8wb8]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8wb8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ligilactobacillus_ruminis_ATCC_25644 Ligilactobacillus ruminis ATCC 25644]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8WB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8WB8 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]] 2.3&#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=8wb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8wb8 OCA], [https://pdbe.org/8wb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8wb8 RCSB], [https://www.ebi.ac.uk/pdbsum/8wb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8wb8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/E7FRT5_9LACO E7FRT5_9LACO] 
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== Publication Abstract from PubMed ==
Sortase-dependent pili are long surface appendages that mediate attachment, colonization and biofilm formation in certain genera and species of Gram-positive bacteria. Ligilactobacillus ruminis is an autochthonous gut commensal that relies on sortase-dependent LrpCBA pili for host adherence and persistence. X-ray crystal structure snapshots of the backbone pilin LrpA were captured in two atypical bent conformations leading to a zigzag morphology in the LrpCBA pilus structure. Small-angle X-ray scattering and structural analysis revealed that LrpA also adopts the typical linear conformation, resulting in an elongated pilus morphology. Various conformational analyses and biophysical experiments helped to demonstrate that a hinge region located at the end of the flexible N-terminal domain of LrpA facilitates a new closure-and-twist motion for assembling dynamic pili during the assembly process and host attachment. Further, the incongruent combination of flexible domain-driven conformational dynamics and rigid isopeptide bond-driven stability observed in the LrpCBA pilus might also extend to the sortase-dependent pili of other bacteria colonizing a host.

The crystal structure of the N-terminal domain of the backbone pilin LrpA reveals a new closure-and-twist motion for assembling dynamic pili in Ligilactobacillus ruminis.,Prajapati A, Palva A, von Ossowski I, Krishnan V Acta Crystallogr D Struct Biol. 2024 Jul 1;80(Pt 7):474-492. doi: , 10.1107/S2059798324005114. Epub 2024 Jun 27. PMID:38935340<ref>PMID:38935340</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Ligilactobacillus ruminis ATCC 25644]]
[[Category: Krishnan V]]
[[Category: Palva A]]
[[Category: Prajapati A]]
[[Category: Von Ossowski I]]