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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
23
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pubmed:dateCreated |
2004-11-19
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pubmed:databankReference |
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pubmed:abstractText |
Lipoic acid is an essential prosthetic group in several metabolic pathways. The biosynthetic pathway of protein lipoylation in Escherichia coli involves gene products of the lip operon. YbeD is a conserved bacterial protein located in the dacA-lipB intergenic region. Here, we report the nuclear magnetic resonance structure of YbeD from E. coli. The structure includes a beta alpha beta beta alpha beta fold with two alpha-helices on one side of a four-strand antiparallel beta-sheet. The beta 2-beta 3 loop shows the highest sequence conservation and is likely functionally important. The beta-sheet surface contains a patch of conserved hydrophobic residues, suggesting a role in protein-protein interactions. YbeD shows striking structural homology to the regulatory domain from d-3-phosphoglycerate dehydrogenase, hinting at a role in the allosteric regulation of lipoic acid biosynthesis or the glycine cleavage system.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-10212987,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-10222208,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-10966480,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-11106496,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-12591875,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-15299354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-1577793,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-1655709,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-1758883,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-3108237,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-3316191,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-4585091,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-4598009,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-4889470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-6986167,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-7719856,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-7812158,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-7881269,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-8002607,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-8206909,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-8444795,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-8744573,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-8771194,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-8798520,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-8902363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-9008363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-9218413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-9268025,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-9367762,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15547281-9614273
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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 |
Dec
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pubmed:issn |
0021-9193
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
186
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8083-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
2004
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pubmed:articleTitle |
Structural similarity of YbeD protein from Escherichia coli to allosteric regulatory domains.
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pubmed:affiliation |
Department of Biochemistry, McGill University, Montreal, Quebec, Canada H3G 1Y6.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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