4g1j

<StructureSection load='4g1j' size='340' side='right' caption='[[4g1j]], [[Resolution|resolution]] 1.75&Aring;' scene=''>

<table><tr><td colspan='2'>[[4g1j]] is a 2 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=4G1J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G1J FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4g1h|4g1h]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SAG0647 ([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=4g1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g1j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g1j RCSB], [http://www.ebi.ac.uk/pdbsum/4g1j PDBsum]</span></td></tr>

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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<references/>

[[Category: Streptococcus agalactiae serogroup v]]

[[Category: Alber, T]]

[[Category: Cozzi, R]]

[[Category: Prigozhin, D M]]

[[Category: Transferase]]