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[[ | ==CRYSTAL STRUCTURE OF SORTASE C-1 (SRTC-1) from Streptococcus pneumoniae== | ||
<StructureSection load='2w1j' size='340' side='right' caption='[[2w1j]], [[Resolution|resolution]] 1.24Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2w1j]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae_tigr4 Streptococcus pneumoniae tigr4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W1J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2W1J FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2w1k|2w1k]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidyltransferase Peptidyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.12 2.3.2.12] </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=2w1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w1j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2w1j RCSB], [http://www.ebi.ac.uk/pdbsum/2w1j PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Streptococcus pneumoniae is a piliated pathogen whose ability to circumvent vaccination and antibiotic treatment strategies is a cause of mortality worldwide. Pili play important roles in pneumococcal infection, but little is known about their biogenesis mechanism or the relationship between components of the pilus-forming machinery, which includes the fiber pilin (RrgB), two minor pilins (RrgA, RrgC), and three sortases (SrtC-1, SrtC-2, SrtC-3). Here we show that SrtC-1 is the main pilus-polymerizing transpeptidase, and electron microscopy analyses of RrgB fibers reconstituted in vitro reveal that they structurally mimic the pneumococcal pilus backbone. Crystal structures of both SrtC-1 and SrtC-3 reveal active sites whose access is controlled by flexible lids, unlike in non-pilus sortases, and suggest that substrate specificity is dictated by surface recognition coupled to lid opening. The distinct structural features of pilus-forming sortases suggest a common pilus biogenesis mechanism that could be exploited for the development of broad-spectrum antibacterials. | |||
Sortase-Mediated Pilus Fiber Biogenesis in Streptococcus pneumoniae.,Manzano C, Contreras-Martel C, El Mortaji L, Izore T, Fenel D, Vernet T, Schoehn G, Di Guilmi AM, Dessen A Structure. 2008 Dec 12;16(12):1838-48. PMID:19081060<ref>PMID:19081060</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Peptidyltransferase]] | [[Category: Peptidyltransferase]] | ||
[[Category: Streptococcus pneumoniae tigr4]] | [[Category: Streptococcus pneumoniae tigr4]] | ||
[[Category: Contreras-Martel, C | [[Category: Contreras-Martel, C]] | ||
[[Category: Dessen, A | [[Category: Dessen, A]] | ||
[[Category: Fenel, D | [[Category: Fenel, D]] | ||
[[Category: Guilmi, A M.Di | [[Category: Guilmi, A M.Di]] | ||
[[Category: Izore, T | [[Category: Izore, T]] | ||
[[Category: Manzano, C | [[Category: Manzano, C]] | ||
[[Category: Mortaji, L El | [[Category: Mortaji, L El]] | ||
[[Category: Schoehn, G | [[Category: Schoehn, G]] | ||
[[Category: Vernet, T | [[Category: Vernet, T]] | ||
[[Category: Pathogenicity]] | [[Category: Pathogenicity]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 11:54, 8 December 2014
CRYSTAL STRUCTURE OF SORTASE C-1 (SRTC-1) from Streptococcus pneumoniaeCRYSTAL STRUCTURE OF SORTASE C-1 (SRTC-1) from Streptococcus pneumoniae
Structural highlights
Publication Abstract from PubMedStreptococcus pneumoniae is a piliated pathogen whose ability to circumvent vaccination and antibiotic treatment strategies is a cause of mortality worldwide. Pili play important roles in pneumococcal infection, but little is known about their biogenesis mechanism or the relationship between components of the pilus-forming machinery, which includes the fiber pilin (RrgB), two minor pilins (RrgA, RrgC), and three sortases (SrtC-1, SrtC-2, SrtC-3). Here we show that SrtC-1 is the main pilus-polymerizing transpeptidase, and electron microscopy analyses of RrgB fibers reconstituted in vitro reveal that they structurally mimic the pneumococcal pilus backbone. Crystal structures of both SrtC-1 and SrtC-3 reveal active sites whose access is controlled by flexible lids, unlike in non-pilus sortases, and suggest that substrate specificity is dictated by surface recognition coupled to lid opening. The distinct structural features of pilus-forming sortases suggest a common pilus biogenesis mechanism that could be exploited for the development of broad-spectrum antibacterials. Sortase-Mediated Pilus Fiber Biogenesis in Streptococcus pneumoniae.,Manzano C, Contreras-Martel C, El Mortaji L, Izore T, Fenel D, Vernet T, Schoehn G, Di Guilmi AM, Dessen A Structure. 2008 Dec 12;16(12):1838-48. PMID:19081060[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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