7ba2: Difference between revisions
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<StructureSection load='7ba2' size='340' side='right'caption='[[7ba2]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='7ba2' size='340' side='right'caption='[[7ba2]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7ba2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[7ba2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sanguinis Streptococcus sanguinis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BA2 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</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=7ba2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ba2 OCA], [https://pdbe.org/7ba2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ba2 RCSB], [https://www.ebi.ac.uk/pdbsum/7ba2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ba2 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=7ba2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ba2 OCA], [https://pdbe.org/7ba2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ba2 RCSB], [https://www.ebi.ac.uk/pdbsum/7ba2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ba2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/A0A0B7GP99_STRSA A0A0B7GP99_STRSA] Required for transformation and DNA binding.[ARBA:ARBA00003988] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 7ba2" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 7ba2" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Pilin 3D structures|Pilin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Streptococcus sanguinis]] | ||
[[Category: | [[Category: Pelicic V]] | ||
[[Category: | [[Category: Sheppard D]] | ||
Latest revision as of 15:24, 1 February 2024
D319A mutant of the PilB minor pilin from Streptococcus sanguinisD319A mutant of the PilB minor pilin from Streptococcus sanguinis
Structural highlights
FunctionA0A0B7GP99_STRSA Required for transformation and DNA binding.[ARBA:ARBA00003988] Publication Abstract from PubMedType IV pili (T4P) are functionally versatile filamentous nanomachines, nearly ubiquitous in prokaryotes. They are predominantly polymers of one major pilin but also contain minor pilins whose functions are often poorly defined and likely to be diverse. Here, we show that the minor pilin PilB from the T4P of Streptococcus sanguinis displays an unusual bimodular three-dimensional structure with a bulky von Willebrand factor A-like (vWA) module "grafted" onto a small pilin module via a short loop. Structural modeling suggests that PilB is only compatible with a localization at the tip of T4P. By performing a detailed functional analysis, we found that 1) the vWA module contains a canonical metal ion-dependent adhesion site, preferentially binding Mg(2+) and Mn(2+), 2) abolishing metal binding has no impact on the structure of PilB or piliation, 3) metal binding is important for S. sanguinis T4P-mediated twitching motility and adhesion to eukaryotic cells, and 4) the vWA module shows an intrinsic binding ability to several host proteins. These findings reveal an elegant yet simple evolutionary tinkering strategy to increase T4P functional versatility by grafting a functional module onto a pilin for presentation by the filaments. This strategy appears to have been extensively used by bacteria, in which modular pilins are widespread and exhibit an astonishing variety of architectures. PilB from Streptococcus sanguinis is a bimodular type IV pilin with a direct role in adhesion.,Raynaud C, Sheppard D, Berry JL, Gurung I, Pelicic V Proc Natl Acad Sci U S A. 2021 Jun 1;118(22). pii: 2102092118. doi:, 10.1073/pnas.2102092118. PMID:34031252[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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