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| | ==Group B Streptococcus Pilus Island 1 Sortase C2== | | ==Group B Streptococcus Pilus Island 1 Sortase C2== |
| - | <StructureSection load='4g1h' size='340' side='right' caption='[[4g1h]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='4g1h' size='340' side='right'caption='[[4g1h]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4g1h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_agalactiae_(serotype_v) Streptococcus agalactiae (serotype v)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G1H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G1H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4g1h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae_serogroup_V Streptococcus agalactiae serogroup V]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G1H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G1H FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4g1j|4g1j]]</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=4g1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g1h OCA], [https://pdbe.org/4g1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g1h RCSB], [https://www.ebi.ac.uk/pdbsum/4g1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g1h ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SAG0648 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216466 Streptococcus agalactiae (serotype V)])</td></tr>
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| - | <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=4g1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g1h OCA], [http://pdbe.org/4g1h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g1h RCSB], [http://www.ebi.ac.uk/pdbsum/4g1h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g1h ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8E0S6_STRA5 Q8E0S6_STRA5] |
| | <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: Alber, T]] | + | [[Category: Large Structures]] |
| - | [[Category: Cozzi, R]] | + | [[Category: Streptococcus agalactiae serogroup V]] |
| - | [[Category: Prigozhin, D M]] | + | [[Category: Alber T]] |
| - | [[Category: Cysteine protease]] | + | [[Category: Cozzi R]] |
| - | [[Category: Extracellular]] | + | [[Category: Prigozhin DM]] |
| - | [[Category: Transferase]]
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| Structural highlights
Function
Q8E0S6_STRA5
Publication Abstract from PubMed
Gram-positive bacteria assemble pili through class C sortase enzymes specialized in polymerizing pilin subunits into covalently linked, high-molecular-weight, elongated structures. Here we report the crystal structures of two class C sortases (SrtC1 and SrtC2) from Group B Streptococcus (GBS) Pilus Island 1. The structures show that both sortases are comprised of two domains: an 8-stranded beta-barrel catalytic core conserved among all sortase family members and a flexible N-terminal region made of two alpha-helices followed by a loop, known as the lid, which acts as a pseudo-substrate. In vitro experiments performed with recombinant SrtC enzymes lacking the N-terminal portion demonstrate that this region of the enzyme is dispensable for catalysis but may have key roles in substrate specificity and regulation. Moreover, in vitro FRET-based assays show that the LPXTG motif common to many sortase substrates is not the sole determinant of sortase C specificity during pilin protein recognition.
Structural basis for group B streptococcus pilus 1 sortases C regulation and specificity.,Cozzi R, Prigozhin D, Rosini R, Abate F, Bottomley MJ, Grandi G, Telford JL, Rinaudo CD, Maione D, Alber T PLoS One. 2012;7(11):e49048. doi: 10.1371/journal.pone.0049048. Epub 2012 Nov 8. PMID:23145064[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cozzi R, Prigozhin D, Rosini R, Abate F, Bottomley MJ, Grandi G, Telford JL, Rinaudo CD, Maione D, Alber T. Structural basis for group B streptococcus pilus 1 sortases C regulation and specificity. PLoS One. 2012;7(11):e49048. doi: 10.1371/journal.pone.0049048. Epub 2012 Nov 8. PMID:23145064 doi:http://dx.doi.org/10.1371/journal.pone.0049048
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