4oq1: Difference between revisions
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==Structure of the Streptococcal ancillary pilin== | |||
<StructureSection load='4oq1' size='340' side='right'caption='[[4oq1]], [[Resolution|resolution]] 1.85Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4oq1]] is a 1 chain structure with sequence from [https://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=4OQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OQ1 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</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=4oq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oq1 OCA], [https://pdbe.org/4oq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oq1 RCSB], [https://www.ebi.ac.uk/pdbsum/4oq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oq1 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0H2UNM0_STRPN A0A0H2UNM0_STRPN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Pili are surface-attached, fibrous virulence factors that play key roles in the pathogenesis process of a number of bacterial agents. Streptococcus pneumoniae is a causative agent of pneumonia and meningitis, and the appearance of drug-resistance organisms has made its treatment challenging, especially in developing countries. Pneumococcus-expressed pili are composed of three structural proteins: RrgB, which forms the polymerized backbone, RrgA, the tip-associated adhesin, and RrgC, which presumably associates the pilus to the bacterial cell wall. Despite the fact that the structures of both RrgA and RrgB were previously known, structural information for RrgC was still lacking, impeding the analysis of a complete model of pilus architecture. Here, we report the structure of RrgC to 1.85 A, and reveal that it is a three-domain molecule stabilized by two intradomain isopeptide bonds. RrgC does not depend on pilus-specific sortases to become attached to the cell wall; instead, it binds the pre-formed pilus to the peptidoglycan by employing the catalytic activity of SrtA. A comprehensive model of the type 1 pilus from S. pneumoniae is also proposed. | |||
Structural basis of pilus anchoring by the ancillary pilin RrgC of Streptococcus pneumoniae.,Shaik MM, Maccagni A, Tourcier G, Di Guilmi AM, Dessen A J Biol Chem. 2014 Apr 21. PMID:24755220<ref>PMID:24755220</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4oq1" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptococcus pneumoniae TIGR4]] | |||
[[Category: Dessen A]] | |||
[[Category: Di Guilmi AM]] | |||
[[Category: Shaik MM]] | |||
Latest revision as of 14:15, 6 November 2024
Structure of the Streptococcal ancillary pilinStructure of the Streptococcal ancillary pilin
Structural highlights
FunctionPublication Abstract from PubMedPili are surface-attached, fibrous virulence factors that play key roles in the pathogenesis process of a number of bacterial agents. Streptococcus pneumoniae is a causative agent of pneumonia and meningitis, and the appearance of drug-resistance organisms has made its treatment challenging, especially in developing countries. Pneumococcus-expressed pili are composed of three structural proteins: RrgB, which forms the polymerized backbone, RrgA, the tip-associated adhesin, and RrgC, which presumably associates the pilus to the bacterial cell wall. Despite the fact that the structures of both RrgA and RrgB were previously known, structural information for RrgC was still lacking, impeding the analysis of a complete model of pilus architecture. Here, we report the structure of RrgC to 1.85 A, and reveal that it is a three-domain molecule stabilized by two intradomain isopeptide bonds. RrgC does not depend on pilus-specific sortases to become attached to the cell wall; instead, it binds the pre-formed pilus to the peptidoglycan by employing the catalytic activity of SrtA. A comprehensive model of the type 1 pilus from S. pneumoniae is also proposed. Structural basis of pilus anchoring by the ancillary pilin RrgC of Streptococcus pneumoniae.,Shaik MM, Maccagni A, Tourcier G, Di Guilmi AM, Dessen A J Biol Chem. 2014 Apr 21. PMID:24755220[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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