View source for 5utt


==SrtA sortase from Actinomyces oris==
<StructureSection load='5utt' size='340' side='right'caption='[[5utt]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5utt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinomyces_oris Actinomyces oris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UTT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UTT 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]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=5utt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5utt OCA], [https://pdbe.org/5utt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5utt RCSB], [https://www.ebi.ac.uk/pdbsum/5utt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5utt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0X8K1J2_9ACTO A0A0X8K1J2_9ACTO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Assembly of pili on the gram-positive bacterial cell wall involves 2 conserved transpeptidase enzymes named sortases: One for polymerization of pilin subunits and another for anchoring pili to peptidoglycan. How this machine controls pilus length and whether pilus length is critical for cell-to-cell interactions remain unknown. We report here in Actinomyces oris, a key colonizer in the development of oral biofilms, that genetic disruption of its housekeeping sortase SrtA generates exceedingly long pili, catalyzed by its pilus-specific sortase SrtC2 that possesses both pilus polymerization and cell wall anchoring functions. Remarkably, the srtA-deficient mutant fails to mediate interspecies interactions, or coaggregation, even though the coaggregation factor CafA is present at the pilus tip. Increasing ectopic expression of srtA in the mutant progressively shortens pilus length and restores coaggregation accordingly, while elevated levels of shaft pilins and SrtC2 produce long pili and block coaggregation by SrtA(+) bacteria. With structural studies, we uncovered 2 key structural elements in SrtA that partake in recognition of pilin substrates and regulate pilus length by inducing the capture and transfer of pilus polymers to the cell wall. Evidently, coaggregation requires proper positioning of the tip adhesin CafA via modulation of pilus length by the housekeeping sortase SrtA.

Cell-to-cell interaction requires optimal positioning of a pilus tip adhesin modulated by gram-positive transpeptidase enzymes.,Chang C, Wu C, Osipiuk J, Siegel SD, Zhu S, Liu X, Joachimiak A, Clubb RT, Das A, Ton-That H Proc Natl Acad Sci U S A. 2019 Sep 3;116(36):18041-18049. doi:, 10.1073/pnas.1907733116. Epub 2019 Aug 19. PMID:31427528<ref>PMID:31427528</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5utt" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Actinomyces oris]]
[[Category: Large Structures]]
[[Category: Anderson WF]]
[[Category: Joachimiak A]]
[[Category: Ma X]]
[[Category: Osipiuk J]]
[[Category: Ton-That H]]