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| | <StructureSection load='4y25' size='340' side='right'caption='[[4y25]], [[Resolution|resolution]] 2.82Å' scene=''> | | <StructureSection load='4y25' size='340' side='right'caption='[[4y25]], [[Resolution|resolution]] 2.82Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4y25]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y25 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4y25]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y25 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pgaA, ycdS, b1024, JW1010 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.821Å</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=4y25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y25 OCA], [https://pdbe.org/4y25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y25 RCSB], [https://www.ebi.ac.uk/pdbsum/4y25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y25 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=4y25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y25 OCA], [https://pdbe.org/4y25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y25 RCSB], [https://www.ebi.ac.uk/pdbsum/4y25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y25 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PGAA_ECOLI PGAA_ECOLI]] Exports the biofilm adhesin polysaccharide poly-beta-1,6-N-acetyl-D-glucosamine (PGA) across the outer membrane. The PGA transported seems to be partially N-deacetylated since N-deacetylation of PGA by PgaB is needed for PGA export through the PgaA porin. Required for the synthesis of the beta-1,6-GlcNAc polysaccharide (PGA or poly-GlcNAc) that seems to serve as a biofilm adhesin.
| + | [https://www.uniprot.org/uniprot/PGAA_ECOLI PGAA_ECOLI] Exports the biofilm adhesin polysaccharide poly-beta-1,6-N-acetyl-D-glucosamine (PGA) across the outer membrane. The PGA transported seems to be partially N-deacetylated since N-deacetylation of PGA by PgaB is needed for PGA export through the PgaA porin. Required for the synthesis of the beta-1,6-GlcNAc polysaccharide (PGA or poly-GlcNAc) that seems to serve as a biofilm adhesin. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: AndolePannuri, A]] | + | [[Category: AndolePannuri A]] |
| - | [[Category: Cao, X]] | + | [[Category: Cao X]] |
| - | [[Category: Huang, Y]] | + | [[Category: Huang Y]] |
| - | [[Category: Lu, X]] | + | [[Category: Lu X]] |
| - | [[Category: Ni, D]] | + | [[Category: Ni D]] |
| - | [[Category: Romeo, T]] | + | [[Category: Romeo T]] |
| - | [[Category: Wang, Y]] | + | [[Category: Wang Y]] |
| - | [[Category: Zhou, H]] | + | [[Category: Zhou H]] |
| - | [[Category: Bacterial polysaccharide]]
| + | |
| - | [[Category: Beta-barrel]]
| + | |
| - | [[Category: Biofilm]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Outer membrane seretin]]
| + | |
| Structural highlights
Function
PGAA_ECOLI Exports the biofilm adhesin polysaccharide poly-beta-1,6-N-acetyl-D-glucosamine (PGA) across the outer membrane. The PGA transported seems to be partially N-deacetylated since N-deacetylation of PGA by PgaB is needed for PGA export through the PgaA porin. Required for the synthesis of the beta-1,6-GlcNAc polysaccharide (PGA or poly-GlcNAc) that seems to serve as a biofilm adhesin.
Publication Abstract from PubMed
The partially de-N-acetylated poly-beta-1,6-N-acetyl-d-glucosamine (dPNAG) polymer serves as an intercellular biofilm adhesin that plays an essential role for the development and maintenance of integrity of biofilms of diverse bacterial species. Translocation of dPNAG across the bacterial outer membrane is mediated by a tetratricopeptide repeat-containing outer membrane protein, PgaA. To understand the molecular basis of dPNAG translocation, we determined the crystal structure of the C-terminal transmembrane domain of PgaA (residues 513-807). The structure reveals that PgaA forms a 16-strand transmembrane beta-barrel, closed by four loops on the extracellular surface. Half of the interior surface of the barrel that lies parallel to the translocation pathway is electronegative, suggesting that the corresponding negatively charged residues may assist the secretion of the positively charged dPNAG polymer. In vivo complementation assays in a pgaA deletion bacterial strain showed that a cluster of negatively charged residues proximal to the periplasm is necessary for biofilm formation. Biochemical analyses further revealed that the tetratricopeptide repeat domain of PgaA binds directly to the N-deacetylase PgaB and is critical for biofilm formation. Our studies support a model in which the positively charged PgaB-bound dPNAG polymer is delivered to PgaA through the PgaA-PgaB interaction and is further targeted to the beta-barrel lumen of PgaA potentially via a charge complementarity mechanism, thus priming the translocation of dPNAG across the bacterial outer membrane.
Structural Basis for Translocation of a Biofilm-supporting Exopolysaccharide across the Bacterial Outer Membrane.,Wang Y, Andole Pannuri A, Ni D, Zhou H, Cao X, Lu X, Romeo T, Huang Y J Biol Chem. 2016 May 6;291(19):10046-57. doi: 10.1074/jbc.M115.711762. Epub 2016, Mar 8. PMID:26957546[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang Y, Andole Pannuri A, Ni D, Zhou H, Cao X, Lu X, Romeo T, Huang Y. Structural Basis for Translocation of a Biofilm-supporting Exopolysaccharide across the Bacterial Outer Membrane. J Biol Chem. 2016 May 6;291(19):10046-57. doi: 10.1074/jbc.M115.711762. Epub 2016, Mar 8. PMID:26957546 doi:http://dx.doi.org/10.1074/jbc.M115.711762
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