5t10: Difference between revisions
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==PelC dodecamer from Paraburkholderia phytofirmans, space group P6== | |||
<StructureSection load='5t10' size='340' side='right'caption='[[5t10]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5t10]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Paraburkholderia_phytofirmans_PsJN Paraburkholderia phytofirmans PsJN]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T10 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]] 2.4987Å</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=5t10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t10 OCA], [https://pdbe.org/5t10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t10 RCSB], [https://www.ebi.ac.uk/pdbsum/5t10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t10 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/B2T2U6_PARPJ B2T2U6_PARPJ] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Secreted polysaccharides are important functional and structural components of bacterial biofilms. The opportunistic pathogen Pseudomonas aeruginosa produces the cationic exopolysaccharide Pel, which protects bacteria from aminoglycoside antibiotics and contributes to biofilm architecture through ionic interactions with extracellular DNA. A bioinformatics analysis of genome databases suggests that gene clusters for Pel biosynthesis are present in >125 bacterial species, yet little is known about how this biofilm exopolysaccharide is synthesized and exported from the cell. In this work, we characterize PelC, an outer membrane lipoprotein essential for Pel production. Crystal structures of PelC from Geobacter metallireducens and Paraburkholderia phytofirmans coupled with structure-guided disulfide cross-linking in P. aeruginosa suggest that PelC assembles into a 12- subunit ring-shaped oligomer. In this arrangement, an aromatic belt in proximity to its lipidation site positions the highly electronegative surface of PelC toward the periplasm. PelC is structurally similar to the Escherichia coli amyloid exporter CsgG; however, unlike CsgG, PelC does not possess membrane-spanning segments required for polymer export across the outer membrane. We show that the multidomain protein PelB with a predicted C-terminal beta-barrel porin localizes to the outer membrane, and propose that PelC functions as an electronegative funnel to guide the positively charged Pel polysaccharide toward an exit channel formed by PelB. Together, our findings provide insight into the unique molecular architecture and export mechanism of the Pel apparatus, a widespread exopolysaccharide secretion system found in environmental and pathogenic bacteria. | |||
Oligomeric lipoprotein PelC guides Pel polysaccharide export across the outer membrane of Pseudomonas aeruginosa.,Marmont LS, Rich JD, Whitney JC, Whitfield GB, Almblad H, Robinson H, Parsek MR, Harrison JJ, Howell PL Proc Natl Acad Sci U S A. 2017 Feb 27. pii: 201613606. doi:, 10.1073/pnas.1613606114. PMID:28242707<ref>PMID:28242707</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5t10" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Paraburkholderia phytofirmans PsJN]] | |||
[[Category: Howell PL]] | |||
[[Category: Marmont LS]] | |||
Latest revision as of 15:52, 4 October 2023
PelC dodecamer from Paraburkholderia phytofirmans, space group P6PelC dodecamer from Paraburkholderia phytofirmans, space group P6
Structural highlights
FunctionPublication Abstract from PubMedSecreted polysaccharides are important functional and structural components of bacterial biofilms. The opportunistic pathogen Pseudomonas aeruginosa produces the cationic exopolysaccharide Pel, which protects bacteria from aminoglycoside antibiotics and contributes to biofilm architecture through ionic interactions with extracellular DNA. A bioinformatics analysis of genome databases suggests that gene clusters for Pel biosynthesis are present in >125 bacterial species, yet little is known about how this biofilm exopolysaccharide is synthesized and exported from the cell. In this work, we characterize PelC, an outer membrane lipoprotein essential for Pel production. Crystal structures of PelC from Geobacter metallireducens and Paraburkholderia phytofirmans coupled with structure-guided disulfide cross-linking in P. aeruginosa suggest that PelC assembles into a 12- subunit ring-shaped oligomer. In this arrangement, an aromatic belt in proximity to its lipidation site positions the highly electronegative surface of PelC toward the periplasm. PelC is structurally similar to the Escherichia coli amyloid exporter CsgG; however, unlike CsgG, PelC does not possess membrane-spanning segments required for polymer export across the outer membrane. We show that the multidomain protein PelB with a predicted C-terminal beta-barrel porin localizes to the outer membrane, and propose that PelC functions as an electronegative funnel to guide the positively charged Pel polysaccharide toward an exit channel formed by PelB. Together, our findings provide insight into the unique molecular architecture and export mechanism of the Pel apparatus, a widespread exopolysaccharide secretion system found in environmental and pathogenic bacteria. Oligomeric lipoprotein PelC guides Pel polysaccharide export across the outer membrane of Pseudomonas aeruginosa.,Marmont LS, Rich JD, Whitney JC, Whitfield GB, Almblad H, Robinson H, Parsek MR, Harrison JJ, Howell PL Proc Natl Acad Sci U S A. 2017 Feb 27. pii: 201613606. doi:, 10.1073/pnas.1613606114. PMID:28242707[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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