rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 7
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pubmed:dateCreated |
2006-7-5
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pubmed:abstractText |
Streptococcus pneumoniae contains a large number of sugar-transport systems and the system responsible for raffinose uptake has recently been identified. The substrate-binding protein component of this system shares strong sequence homology with the multiple sugar metabolism substrate-binding protein MsmE from S. mutans and contains a lipoprotein-attachment site at cysteine residue 23. A truncated form (residues 24-419) of RafE from S. pneumoniae was cloned and overexpressed in Escherichia coli. Native and selenomethionine-labelled protein have been crystallized in the hexagonal space group P6(1)22. Diffraction data have been successfully phased to 2.90 angstroms using Se SAD data and model building is in progress.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1744-3091
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
62
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
676-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16820692-Bacterial Proteins,
pubmed-meshheading:16820692-Binding Sites,
pubmed-meshheading:16820692-Cloning, Molecular,
pubmed-meshheading:16820692-Crystallography,
pubmed-meshheading:16820692-Escherichia coli,
pubmed-meshheading:16820692-Lipoproteins,
pubmed-meshheading:16820692-Raffinose,
pubmed-meshheading:16820692-Recombinant Proteins,
pubmed-meshheading:16820692-Selenomethionine,
pubmed-meshheading:16820692-Streptococcus pneumoniae,
pubmed-meshheading:16820692-X-Ray Diffraction
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pubmed:year |
2006
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pubmed:articleTitle |
Purification, crystallization and preliminary X-ray diffraction analysis of RafE, a sugar-binding lipoprotein from Streptococcus pneumoniae.
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pubmed:affiliation |
Department of Chemistry and WestCHEM, Glasgow Biomedical Research Centre (GBRC), University of Glasgow, 120 University Place, Glasgow G12 8TA, Scotland. neison@chem.gla.ac.uk
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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