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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1995-10-26
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D90259,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M24890,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/P14326,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/P15304,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/P23872,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/P24484,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/Q01109,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/Q05469,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S20686,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X71598,
http://linkedlifedata.com/resource/pubmed/xref/PIR/D90259,
http://linkedlifedata.com/resource/pubmed/xref/PIR/M24890,
http://linkedlifedata.com/resource/pubmed/xref/PIR/P14326,
http://linkedlifedata.com/resource/pubmed/xref/PIR/P15304,
http://linkedlifedata.com/resource/pubmed/xref/PIR/P23872,
http://linkedlifedata.com/resource/pubmed/xref/PIR/P24484,
http://linkedlifedata.com/resource/pubmed/xref/PIR/Q01109,
http://linkedlifedata.com/resource/pubmed/xref/PIR/Q05469,
http://linkedlifedata.com/resource/pubmed/xref/PIR/S20686,
http://linkedlifedata.com/resource/pubmed/xref/PIR/X71598,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/D90259,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/M24890,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P14326,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P15304,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P23872,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P24484,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/Q01109,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/Q05469,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/S20686,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/X71598
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pubmed:abstractText |
The primary sequence of esterases from Acinetobacter lwoffii RAG-1 and A. calcoaceticus BD413 were compared with linearized structural sequences of two hundred proteins selected from Brookhaven Protein DataBank using a modified version of the Bowie et al. algorithm [3]. Significant structural homology was found to alpha/beta proteins and specifically to those with the alpha/beta-hydrolase fold for which the crystal structure was reported. No such homology was detected using common primary sequence alignment programs such as FASTA or BLAST.
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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 |
Sep
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
371
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
231-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7556598-Acinetobacter,
pubmed-meshheading:7556598-Acinetobacter calcoaceticus,
pubmed-meshheading:7556598-Algorithms,
pubmed-meshheading:7556598-Amino Acid Sequence,
pubmed-meshheading:7556598-Animals,
pubmed-meshheading:7556598-Bacterial Proteins,
pubmed-meshheading:7556598-Esterases,
pubmed-meshheading:7556598-Humans,
pubmed-meshheading:7556598-Hydrolases,
pubmed-meshheading:7556598-Membrane Proteins,
pubmed-meshheading:7556598-Molecular Sequence Data,
pubmed-meshheading:7556598-Protein Folding,
pubmed-meshheading:7556598-Protein Structure, Tertiary,
pubmed-meshheading:7556598-Sequence Homology, Amino Acid
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pubmed:year |
1995
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pubmed:articleTitle |
Detection of alpha/beta-hydrolase fold in the cell surface esterases of Acinetobacter species using an analysis of 3D profiles.
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pubmed:affiliation |
Department of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Ramat-Aviv, Israel.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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