Source:http://linkedlifedata.com/resource/pubmed/id/11196648
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6817
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pubmed:dateCreated |
2001-1-22
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pubmed:databankReference | |
pubmed:abstractText |
Staphylococcus aureus is a major human pathogen, the potency of which can be attributed to the regulated expression of an impressive array of virulence determinants. A key pleiotropic transcriptional regulator of these virulence factors is SarA, which is encoded by the sar (staphylococcal accessory regulator) locus. SarA was characterized initially as an activator of a second virulence regulatory locus, agr, through its interaction with a series of heptad repeats (AGTTAAG) within the agr promoter. Subsequent DNA-binding studies have revealed that SarA binds readily to multiple AT-rich sequences of variable lengths. Here we describe the crystal structure of SarA and a SarA-DNA complex at resolutions of 2.50 A and 2.95 A, respectively. SarA has a fold consisting of a four-helix core region and 'inducible regions' comprising a beta-hairpin and a carboxy-terminal loop. On binding DNA, the inducible regions undergo marked conformational changes, becoming part of extended and distorted alpha-helices, which encase the DNA. SarA recognizes an AT-rich site in which the DNA is highly overwound and adopts a D-DNA-like conformation by indirect readout. These structures thus provide insight into SarA-mediated transcription regulation.
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pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SarA protein, bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0028-0836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
409
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
215-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11196648-Bacterial Proteins,
pubmed-meshheading:11196648-Crystallography, X-Ray,
pubmed-meshheading:11196648-DNA, Bacterial,
pubmed-meshheading:11196648-DNA-Binding Proteins,
pubmed-meshheading:11196648-Gene Expression Regulation, Bacterial,
pubmed-meshheading:11196648-Models, Molecular,
pubmed-meshheading:11196648-Protein Binding,
pubmed-meshheading:11196648-Protein Conformation,
pubmed-meshheading:11196648-Staphylococcus aureus,
pubmed-meshheading:11196648-Trans-Activators,
pubmed-meshheading:11196648-Virulence
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pubmed:year |
2001
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pubmed:articleTitle |
Crystal structures of SarA, a pleiotropic regulator of virulence genes in S. aureus.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, Portland 97201-3098, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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