Linked Life Data

16820692

Source:http://linkedlifedata.com/resource/pubmed/id/16820692

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pubmed-article:16820692pubmed:dateCreated2006-7-5lld:pubmed
pubmed-article:16820692pubmed:abstractTextStreptococcus 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.lld:pubmed
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pubmed-article:16820692pubmed:authorpubmed-author:MitchellTimot...lld:pubmed
pubmed-article:16820692pubmed:authorpubmed-author:IsaacsNeil...lld:pubmed
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pubmed-article:16820692pubmed:pagination676-9lld:pubmed
pubmed-article:16820692pubmed:dateRevised2009-11-18lld:pubmed
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pubmed-article:16820692pubmed:year2006lld:pubmed
pubmed-article:16820692pubmed:articleTitlePurification, crystallization and preliminary X-ray diffraction analysis of RafE, a sugar-binding lipoprotein from Streptococcus pneumoniae.lld:pubmed
pubmed-article:16820692pubmed:affiliationDepartment of Chemistry and WestCHEM, Glasgow Biomedical Research Centre (GBRC), University of Glasgow, 120 University Place, Glasgow G12 8TA, Scotland. neison@chem.gla.ac.uklld:pubmed
pubmed-article:16820692pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:16820692pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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