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| | ==The crystal structure of Streptococcus pneumoniae Sortase C provides novel insights into catalysis as well as pilin substrate specificity== | | ==The crystal structure of Streptococcus pneumoniae Sortase C provides novel insights into catalysis as well as pilin substrate specificity== |
| - | <StructureSection load='3g66' size='340' side='right' caption='[[3g66]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='3g66' size='340' side='right'caption='[[3g66]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3g66]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"diplococcus_pneumoniae"_(klein_1884)_weichselbaum_1886 "diplococcus pneumoniae" (klein 1884) weichselbaum 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G66 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3G66 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3g66]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G66 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G66 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</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]] 1.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3g69|3g69]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SP_0467, srtC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1313 "Diplococcus pneumoniae" (Klein 1884) Weichselbaum 1886])</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=3g66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g66 OCA], [https://pdbe.org/3g66 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g66 RCSB], [https://www.ebi.ac.uk/pdbsum/3g66 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g66 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=3g66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g66 OCA], [http://pdbe.org/3g66 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3g66 RCSB], [http://www.ebi.ac.uk/pdbsum/3g66 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3g66 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A7KT63_STREE A7KT63_STREE] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Achour, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Dessen, A]] | + | [[Category: Streptococcus pneumoniae]] |
| - | [[Category: Falker, S]] | + | [[Category: Achour A]] |
| - | [[Category: Henriques-Normark, B]] | + | [[Category: Dessen A]] |
| - | [[Category: Madhurantakam, C]] | + | [[Category: Falker S]] |
| - | [[Category: Manzano, C]] | + | [[Category: Henriques-Normark B]] |
| - | [[Category: Neiers, F]] | + | [[Category: Madhurantakam C]] |
| - | [[Category: Normark, S]] | + | [[Category: Manzano C]] |
| - | [[Category: Pilus]]
| + | [[Category: Neiers F]] |
| - | [[Category: S. pneumoniae]]
| + | [[Category: Normark S]] |
| - | [[Category: Sortase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
A7KT63_STREE
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The respiratory tract pathogen Streptococcus pneumoniae is a primary cause of morbidity and mortality worldwide. Pili enhance initial adhesion as well as the capacity of pneumococci to cause pneumonia and bacteremia. Pilus-associated sortases (SrtB, SrtC, and SrtD) are involved in the biogenesis of pneumococcal pili, composed of repeating units of RrgB that create the stalk to which the RrgA adhesin and the preferential pilus tip subunit RrgC are covalently associated. Using single sortase-expressing strains, we demonstrate that both pilin-polymerizing sortases SrtB and SrtC can covalently link pili to the peptidoglycan cell wall, a property shared with the non-pilus-polymerizing enzyme SrtD and the housekeeping sortase SrtA. Comparative analysis of the crystal structures of S. pneumoniae SrtC and SrtB revealed structural differences explaining the incapacity of SrtC, but not of SrtB, to incorporate RrgC into the pilus. Accordingly, site-directed mutagenesis of Thr(160) in SrtB to an arginine as in SrtC (Arg(160)) partially converted its substrate specificity into that of SrtC. Solving two crystal structures for SrtC suggests that an opening of a flexible lid and a concomitant cysteine rotation are important for catalysis and the activation of the catalytic cysteine of pilus-associated sortases.
Two crystal structures of pneumococcal pilus sortase C provide novel insights into catalysis and substrate specificity.,Neiers F, Madhurantakam C, Falker S, Manzano C, Dessen A, Normark S, Henriques-Normark B, Achour A J Mol Biol. 2009 Oct 30;393(3):704-16. Epub 2009 Aug 31. PMID:19729023[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Neiers F, Madhurantakam C, Falker S, Manzano C, Dessen A, Normark S, Henriques-Normark B, Achour A. Two crystal structures of pneumococcal pilus sortase C provide novel insights into catalysis and substrate specificity. J Mol Biol. 2009 Oct 30;393(3):704-16. Epub 2009 Aug 31. PMID:19729023 doi:10.1016/j.jmb.2009.08.058
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