This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4g1h

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:24, 1 March 2024) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
 +
==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]] 1.80&Aring;' scene=''>
+
<StructureSection load='4g1h' size='340' side='right'caption='[[4g1h]], [[Resolution|resolution]] 1.80&Aring;' 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_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>
+
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4g1j|4g1j]]</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='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'>[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='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>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/Q8E0S6_STRA5 Q8E0S6_STRA5]
-
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>
+
-
</div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Streptococcus agalactiae serogroup v]]
+
[[Category: Large Structures]]
-
[[Category: Alber, T]]
+
[[Category: Streptococcus agalactiae serogroup V]]
-
[[Category: Cozzi, R]]
+
[[Category: Alber T]]
-
[[Category: Prigozhin, D M]]
+
[[Category: Cozzi R]]
-
[[Category: Cysteine protease]]
+
[[Category: Prigozhin DM]]
-
[[Category: Extracellular]]
+
-
[[Category: Transferase]]
+

Current revision

Group B Streptococcus Pilus Island 1 Sortase C2

PDB ID 4g1h

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools