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rdf:type |
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lifeskim:mentions |
umls-concept:C0004651,
umls-concept:C1336789,
umls-concept:C1514562,
umls-concept:C1705273,
umls-concept:C1705274,
umls-concept:C1705275,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C1883254,
umls-concept:C2827501
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pubmed:issue |
5
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pubmed:dateCreated |
1984-5-2
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pubmed:abstractText |
The amino-terminal domain of the phage 434 repressor forms cocrystals with a synthetic phage 434 operator. The cocrystals diffract to at least 4 A, and x-ray crystallographic analysis of them is in progress. An analysis of the packing in the cocrystals shows that complexes consisting of dimers of amino-terminal domain bound specifically to operators are stacked end to end in longer protein-DNA rods parallel to the unit cell body diagonals. The DNA in the complexes has 10.5 base pairs per turn and a rise per base of 3.26 A--values consistent with B-form DNA--indicating that DNA is neither unwound nor overwound by bound repressor. The packing analysis suggests an approach that might facilitate the cocrystallization of other DNA-binding proteins with the DNA they recognize.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-16068162,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-217408,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-287002,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-438218,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-4514322,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-4609322,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-6212926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-6213863,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-6261152,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-6265793,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-6265794,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-6286819,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-6297782,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-629949,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-6363212,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-6444544,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-6452580,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-6457992,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-6887256,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-6896364,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-6897265,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-7027256,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-7071593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-7088190,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6369323-7372662
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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 |
Mar
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
81
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1307-11
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:6369323-Base Composition,
pubmed-meshheading:6369323-Coliphages,
pubmed-meshheading:6369323-Crystallization,
pubmed-meshheading:6369323-Escherichia coli,
pubmed-meshheading:6369323-Models, Molecular,
pubmed-meshheading:6369323-Nucleic Acid Conformation,
pubmed-meshheading:6369323-Oligodeoxyribonucleotides,
pubmed-meshheading:6369323-Oligonucleotides,
pubmed-meshheading:6369323-Operon,
pubmed-meshheading:6369323-Protein Binding,
pubmed-meshheading:6369323-Protein Conformation,
pubmed-meshheading:6369323-Repressor Proteins,
pubmed-meshheading:6369323-Transcription Factors,
pubmed-meshheading:6369323-X-Ray Diffraction
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pubmed:year |
1984
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pubmed:articleTitle |
Cocrystals of the DNA-binding domain of phage 434 repressor and a synthetic phage 434 operator.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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