rdf:type |
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lifeskim:mentions |
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pubmed:issue |
18
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pubmed:dateCreated |
1988-10-13
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pubmed:abstractText |
The three-dimensional structure of the medium-chain acyl-CoA dehydrogenase (EC 1.3.99.3) from pig liver mitochondria has been determined to 3.0-A resolution by the x-ray diffraction method. The enzyme is a tetramer of four identical 43-kDa subunits and contains one equivalent of flavin adenine dinucleotide (FAD) per subunit. The polypeptide is folded into three domains. The N-terminal and the C-terminal domains are composed mainly of alpha-helices, and the middle domain is packed with orthogonal beta-sheets. The FAD has an extended conformation: the flavin ring lies between the N-terminal and the beta-sheet domains, and the adenine moiety is found at the junction between the C-terminal and the beta-sheet domains of one subunit and the C-terminal domain of a neighboring subunit. The polypeptide chain folding near the FAD binding site is different from those observed in other flavoproteins, such as glutathione reductase and glycolate oxidase.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/3413116-1168197,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3413116-13130521,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3413116-13295225,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3413116-13319294,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3413116-16593616,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3413116-25387,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3413116-2934605,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3413116-3035565,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3413116-3085707,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3413116-3554243,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3413116-3611054,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3413116-3771568,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3413116-3801393,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/3413116-3968065,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3413116-40036,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3413116-4079800,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3413116-4084503,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/3413116-6699019,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/3413116-7459327,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3413116-925004
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0027-8424
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
85
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6677-81
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pubmed:dateRevised |
2010-9-9
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pubmed:meshHeading |
pubmed-meshheading:3413116-Acyl-CoA Dehydrogenases,
pubmed-meshheading:3413116-Animals,
pubmed-meshheading:3413116-Crystallography,
pubmed-meshheading:3413116-Flavin-Adenine Dinucleotide,
pubmed-meshheading:3413116-Mitochondria, Liver,
pubmed-meshheading:3413116-Models, Molecular,
pubmed-meshheading:3413116-Protein Conformation,
pubmed-meshheading:3413116-Swine,
pubmed-meshheading:3413116-X-Ray Diffraction
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pubmed:year |
1988
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pubmed:articleTitle |
Structure of the medium-chain acyl-CoA dehydrogenase from pig liver mitochondria at 3-A resolution.
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pubmed:affiliation |
Department of Biochemistry, Medical College of Wisconsin, Milwaukee 53226.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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