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==Crystal structure of shaft pilin spaA from Lactobacillus rhamnosus GG - E269A mutant== | |||
<StructureSection load='5hdl' size='340' side='right' caption='[[5hdl]], [[Resolution|resolution]] 2.39Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5hdl]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HDL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HDL FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5f44|5f44]], [[5faa|5faa]], [[5fgs|5fgs]], [[5fgr|5fgr]], [[5fie|5fie]], [[5hbb|5hbb]], [[5hts|5hts]], [[5j4m|5j4m]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5hdl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hdl OCA], [http://pdbe.org/5hdl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hdl RCSB], [http://www.ebi.ac.uk/pdbsum/5hdl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hdl ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Thus far, all solved structures of pilin-proteins comprising sortase-assembled pili are from pathogenic genera and species. Here, we present the first crystal structure of a pilin subunit (SpaA) from a non-pathogen host (Lactobacillus rhamnosus GG). SpaA consists of two tandem CnaB-type domains, each with an isopeptide bond and E-box motif. Intriguingly, while the isopeptide bond in the N-terminal domain forms between lysine and asparagine, the one in the C-terminal domain atypically involves aspartate. We also solved crystal structures of mutant proteins where residues implicated in forming isopeptide bonds were replaced. Expectedly, the E-box-substituted E139A mutant lacks an isopeptide bond in the N-terminal domain. However, the C-terminal E269A substitution gave two structures; one of both domains with their isopeptide bonds present, and another of only the N-terminal domain, but with an unformed isopeptide bond and significant conformational changes. This latter crystal structure has never been observed for any other Gram-positive pilin. Notably, the C-terminal isopeptide bond still forms in D295N-substituted SpaA, irrespective of E269 being present or absent. Although E-box mutations affect SpaA proteolytic and thermal stability, a cumulative effect perturbing normal pilus polymerization was unobserved. A model showing the polymerized arrangement of SpaA within the SpaCBA pilus is proposed. | |||
New insights about pilus formation in gut-adapted Lactobacillus rhamnosus GG from the crystal structure of the SpaA backbone-pilin subunit.,Chaurasia P, Pratap S, von Ossowski I, Palva A, Krishnan V Sci Rep. 2016 Jun 28;6:28664. doi: 10.1038/srep28664. PMID:27349405<ref>PMID:27349405</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 5hdl" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Chaurasia, P]] | |||
[[Category: Krishnan, V]] | [[Category: Krishnan, V]] | ||
[[Category: | [[Category: Ossowski, I von]] | ||
[[Category: Palva, A]] | [[Category: Palva, A]] | ||
[[Category: Pratap, S]] | |||
[[Category: Adhesin]] | |||
[[Category: Cell adhesion]] | |||
[[Category: Isopeptide]] | |||
[[Category: Pilin]] | |||
[[Category: Probiotic]] | |||
[[Category: Spaa]] | |||
[[Category: Spacba pili]] | |||
Revision as of 18:10, 26 July 2016
Crystal structure of shaft pilin spaA from Lactobacillus rhamnosus GG - E269A mutantCrystal structure of shaft pilin spaA from Lactobacillus rhamnosus GG - E269A mutant
Structural highlights
Publication Abstract from PubMedThus far, all solved structures of pilin-proteins comprising sortase-assembled pili are from pathogenic genera and species. Here, we present the first crystal structure of a pilin subunit (SpaA) from a non-pathogen host (Lactobacillus rhamnosus GG). SpaA consists of two tandem CnaB-type domains, each with an isopeptide bond and E-box motif. Intriguingly, while the isopeptide bond in the N-terminal domain forms between lysine and asparagine, the one in the C-terminal domain atypically involves aspartate. We also solved crystal structures of mutant proteins where residues implicated in forming isopeptide bonds were replaced. Expectedly, the E-box-substituted E139A mutant lacks an isopeptide bond in the N-terminal domain. However, the C-terminal E269A substitution gave two structures; one of both domains with their isopeptide bonds present, and another of only the N-terminal domain, but with an unformed isopeptide bond and significant conformational changes. This latter crystal structure has never been observed for any other Gram-positive pilin. Notably, the C-terminal isopeptide bond still forms in D295N-substituted SpaA, irrespective of E269 being present or absent. Although E-box mutations affect SpaA proteolytic and thermal stability, a cumulative effect perturbing normal pilus polymerization was unobserved. A model showing the polymerized arrangement of SpaA within the SpaCBA pilus is proposed. New insights about pilus formation in gut-adapted Lactobacillus rhamnosus GG from the crystal structure of the SpaA backbone-pilin subunit.,Chaurasia P, Pratap S, von Ossowski I, Palva A, Krishnan V Sci Rep. 2016 Jun 28;6:28664. doi: 10.1038/srep28664. PMID:27349405[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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