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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2006-5-22
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pubmed:databankReference |
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pubmed:abstractText |
Secretion via the type II secretion pathway in Gram-negative bacteria often relies crucially on steric chaperones in the periplasm. Here, we report the crystal structure of the soluble form of a lipase-specific foldase (Lif) from Burkholderia glumae in complex with its cognate lipase. The structure reveals how Lif uses a novel alpha-helical scaffold to embrace lipase, thereby creating an unusually extensive folding platform.
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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 |
Apr
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pubmed:issn |
1545-9993
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
374-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16518399-Bacterial Proteins,
pubmed-meshheading:16518399-Burkholderia,
pubmed-meshheading:16518399-Lipase,
pubmed-meshheading:16518399-Models, Molecular,
pubmed-meshheading:16518399-Molecular Chaperones,
pubmed-meshheading:16518399-Multiprotein Complexes,
pubmed-meshheading:16518399-Protein Folding,
pubmed-meshheading:16518399-Protein Structure, Secondary,
pubmed-meshheading:16518399-Substrate Specificity
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pubmed:year |
2006
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pubmed:articleTitle |
Structure of a membrane-based steric chaperone in complex with its lipase substrate.
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pubmed:affiliation |
Department of Molecular and Cellular Interactions, Flanders Interuniversity Institute for Biotechnology (VIB) and Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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