rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2009-3-23
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pubmed:abstractText |
The crystal structure of the H. influenzae YfeU protein, was determined at 1.90 A resolution using multi-wavelength anomalous diffraction. YfeU belongs to a very large conserved family of proteins found mainly in bacteria but also in archaea and eukaryota. The protein is a homolog of eukaryotic glucokinase regulator and is predicted to be a sugar phosphate isomerase or aminotransferase. Here we describe the structure of YfeU and discuss the possible function as an etherase possibly involved in peptidoglycan recycling.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19234762-10091662,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19234762-10329779,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19234762-9757107
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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 |
1570-0267
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
10
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
151-6
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pubmed:dateRevised |
2011-9-26
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pubmed:meshHeading |
pubmed-meshheading:19234762-Amino Acid Sequence,
pubmed-meshheading:19234762-Bacterial Proteins,
pubmed-meshheading:19234762-Binding Sites,
pubmed-meshheading:19234762-Crystallography, X-Ray,
pubmed-meshheading:19234762-Haemophilus influenzae,
pubmed-meshheading:19234762-Models, Molecular,
pubmed-meshheading:19234762-Molecular Sequence Data,
pubmed-meshheading:19234762-Peptidoglycan,
pubmed-meshheading:19234762-Protein Conformation,
pubmed-meshheading:19234762-Protein Folding,
pubmed-meshheading:19234762-Sequence Alignment
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pubmed:year |
2009
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pubmed:articleTitle |
Crystal structure of YfeU protein from Haemophilus influenzae: a predicted etherase involved in peptidoglycan recycling.
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pubmed:affiliation |
Midwest Center for Structural Genomics and Structural Biology Center, Biosciences, Argonne National Laboratory, Argonne, IL 60439, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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