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3rbi

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Current revision (10:53, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3rbi' size='340' side='right'caption='[[3rbi]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='3rbi' size='340' side='right'caption='[[3rbi]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3rbi]] is a 2 chain structure with sequence from [https://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=3RBI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RBI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3rbi]] is a 2 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=3RBI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RBI FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3rbj|3rbj]], [[3rbk|3rbk]], [[3rcc|3rcc]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SAG0647, srtC1 (SAG0647) ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3rbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rbi OCA], [https://pdbe.org/3rbi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rbi RCSB], [https://www.ebi.ac.uk/pdbsum/3rbi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rbi ProSAT]</span></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=3rbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rbi OCA], [https://pdbe.org/3rbi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rbi RCSB], [https://www.ebi.ac.uk/pdbsum/3rbi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rbi ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q8E0S7_STRA5 Q8E0S7_STRA5]
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The assembly of pili on the cell wall of Gram-positive bacteria requires transpeptidase enzymes called sortases. In Streptococcus agalactiae, the PI-1 pilus island of strain 2603V/R encodes two pilus-specific sortases (SrtC1 and SrtC2) and three pilins (GBS80, GBS52 and GBS104). Although either pilus-specific sortase is sufficient for the polymerization of the major pilin, GBS80, incorporation of the minor pilins GBS52 and GBS104 into the pilus structure requires SrtC1 and SrtC2, respectively. The S. agalactiae housekeeping sortase, SrtA, whose gene is present at a different location and does not catalyze pilus polymerization, was shown to be involved in cell wall anchoring of pilus polymers. To understand the structural basis of sortases involved in such diverse functions, we determined the crystal structures of S. agalactiae SrtC1 and SrtA. Both enzymes are made of an eight-stranded beta-barrel core with variations in their active site architecture. SrtA exhibits a catalytic triad arrangement similar to that in Streptococcus pyogenes SrtA but different from that in Staphylococcus aureus SrtA. In contrast, the SrtC1 enzyme contains an N-terminal helical domain and a 'lid' in its putative active site, which is similar to that seen in Streptococcus pneumoniae pilus-specific sortases, although with subtle differences in positioning and composition. To understand the effect of such differences on substrate recognition, we have also determined the crystal structure of a SrtC1 mutant, in which the conserved DP(W/F/Y) motif was replaced with the sorting signal motif of GBS80, IPNTG. By comparing the structures of WT wild type SrtA and SrtC1 and the 'lid' mutant of SrtC1, we propose that structural elements within the active site and the lid may be important for defining the role of specific sortase in pili biogenesis.
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Structural differences between the Streptococcus agalactiae housekeeping and pilus-specific sortases: SrtA and SrtC1.,Khare B, Krishnan V, Rajashankar KR, I-Hsiu H, Xin M, Ton-That H, Narayana SV PLoS One. 2011;6(8):e22995. Epub 2011 Aug 30. PMID:21912586<ref>PMID:21912586</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3rbi" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Khare, B]]
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[[Category: Streptococcus agalactiae serogroup V]]
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[[Category: Narayana, S V.L]]
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[[Category: Khare B]]
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[[Category: Beta-barrel]]
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[[Category: Narayana SVL]]
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[[Category: Class c sortase]]
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[[Category: Hydrolase]]
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[[Category: Pili biogenesis]]
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[[Category: Sortase fold]]
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Current revision

The Type III Crystal Structure of Streptococcus agalactiae Sortase C1

PDB ID 3rbi

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