Source:http://linkedlifedata.com/resource/pubmed/id/19081060
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
2008-12-16
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0969-2126
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1838-48
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pubmed:meshHeading |
pubmed-meshheading:19081060-Amino Acid Sequence,
pubmed-meshheading:19081060-Bacterial Proteins,
pubmed-meshheading:19081060-Binding Sites,
pubmed-meshheading:19081060-Fimbriae, Bacterial,
pubmed-meshheading:19081060-Fimbriae Proteins,
pubmed-meshheading:19081060-Models, Molecular,
pubmed-meshheading:19081060-Molecular Sequence Data,
pubmed-meshheading:19081060-Mutation,
pubmed-meshheading:19081060-Protein Binding,
pubmed-meshheading:19081060-Sequence Homology, Amino Acid,
pubmed-meshheading:19081060-Streptococcus pneumoniae
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pubmed:year |
2008
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pubmed:articleTitle |
Sortase-mediated pilus fiber biogenesis in Streptococcus pneumoniae.
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pubmed:affiliation |
Laboratoire des Protéines Membranaires, Institut de Biologie Structurale Jean-Pierre Ebel, UMR 5075 (CEA, CNRS, UJF, PSB), 41 rue Jules Horowitz, F-38027 Grenoble, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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