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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1987-11-12
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pubmed:abstractText |
The structure of a C-terminal fragment of the ribosomal protein L7/L12 from Escherichia coli has been refined using crystallographic data to 1.7 A resolution. The R-value is 17.4%. Six residues at the N terminus are too disordered in the structure to be localized. These residues are probably part of a hinge in the complete L7/L12 molecule. The possibility that a 2-fold crystallographic axis is a molecular 2-fold axis is discussed. A patch of invariant residues on the surface of the dimer is probably involved in functional interactions with elongation factors.
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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 |
Jun
|
pubmed:issn |
0022-2836
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
5
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pubmed:volume |
195
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
555-79
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3309338-Amino Acid Sequence,
pubmed-meshheading:3309338-Bacterial Proteins,
pubmed-meshheading:3309338-Crystallography,
pubmed-meshheading:3309338-Escherichia coli,
pubmed-meshheading:3309338-Hydrogen Bonding,
pubmed-meshheading:3309338-Models, Molecular,
pubmed-meshheading:3309338-Protein Conformation,
pubmed-meshheading:3309338-Ribosomal Proteins
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pubmed:year |
1987
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pubmed:articleTitle |
Structure of the C-terminal domain of the ribosomal protein L7/L12 from Escherichia coli at 1.7 A.
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pubmed:affiliation |
Institute of Molecular Biology, University of Uppsala, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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