4g1h
From Proteopedia
(Difference between revisions)
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- | [[ | + | ==Group B Streptococcus Pilus Island 1 Sortase C2== |
+ | <StructureSection load='4g1h' size='340' side='right' caption='[[4g1h]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4g1h]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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> | ||
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4g1j|4g1j]]</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 serogroup V])</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=4g1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g1h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g1h RCSB], [http://www.ebi.ac.uk/pdbsum/4g1h PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == 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<ref>PMID:23145064</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | == | + | __TOC__ |
- | + | </StructureSection> | |
[[Category: Streptococcus agalactiae serogroup v]] | [[Category: Streptococcus agalactiae serogroup v]] | ||
- | [[Category: Alber, T | + | [[Category: Alber, T]] |
- | [[Category: Cozzi, R | + | [[Category: Cozzi, R]] |
- | [[Category: Prigozhin, D M | + | [[Category: Prigozhin, D M]] |
[[Category: Cysteine protease]] | [[Category: Cysteine protease]] | ||
[[Category: Extracellular]] | [[Category: Extracellular]] | ||
[[Category: Transferase]] | [[Category: Transferase]] |
Revision as of 17:16, 9 December 2014
Group B Streptococcus Pilus Island 1 Sortase C2
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