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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
23
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pubmed:dateCreated |
1985-1-10
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pubmed:abstractText |
An electron density map of trimethylamine dehydrogenase has been calculated at 6.0-A resolution. Protein phases were based on two isomorphous mercury derivatives with similar binding properties, and on anomalous scattering measurements. The map has been averaged about the noncrystallographic 2-fold axis, plotted on transparent sheets and used to construct a wooden model. The elipsoidal dimer has a large inter-subunit interface. Each subunit appears to contain three closely associated domains with the iron-sulfur cluster located between two of them. The map suggests an alpha/beta-structure for two of the domains and a large helix content for the third.
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pubmed:grant | |
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 |
Dec
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
259
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14458-62
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:6501301-Bacteria,
pubmed-meshheading:6501301-Binding Sites,
pubmed-meshheading:6501301-Macromolecular Substances,
pubmed-meshheading:6501301-Models, Molecular,
pubmed-meshheading:6501301-Oxidoreductases, N-Demethylating,
pubmed-meshheading:6501301-Protein Binding,
pubmed-meshheading:6501301-Protein Conformation,
pubmed-meshheading:6501301-X-Ray Diffraction
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pubmed:year |
1984
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pubmed:articleTitle |
Molecular structure of trimethylamine dehydrogenase from the bacterium W3A1 at 6.0-A resolution.
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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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