rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
2
|
pubmed:dateCreated |
1993-9-3
|
pubmed:abstractText |
The first three-dimensional structure of a DNA methyltransferase is presented. The crystal structure of the DNA (cytosine-5)-methyltransferase, M.HhaI (recognition sequence: GCGC), complexed with S-adenosyl-L-methionine has been determined and refined at 2.5 A resolution. The core of the structure is dominated by sequence motifs conserved among all DNA (cytosine-5)-methyltransferases, and these are responsible for cofactor binding and methyltransferase function.
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pubmed:grant |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
0092-8674
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
30
|
pubmed:volume |
74
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
299-307
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pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
pubmed-meshheading:8343957-Amino Acid Sequence,
pubmed-meshheading:8343957-Conserved Sequence,
pubmed-meshheading:8343957-DNA,
pubmed-meshheading:8343957-DNA-Cytosine Methylases,
pubmed-meshheading:8343957-Haemophilus,
pubmed-meshheading:8343957-Models, Molecular,
pubmed-meshheading:8343957-Molecular Sequence Data,
pubmed-meshheading:8343957-Protein Structure, Secondary,
pubmed-meshheading:8343957-Protein Structure, Tertiary,
pubmed-meshheading:8343957-Recombinant Proteins,
pubmed-meshheading:8343957-S-Adenosylmethionine,
pubmed-meshheading:8343957-Sequence Homology, Amino Acid,
pubmed-meshheading:8343957-X-Ray Diffraction
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pubmed:year |
1993
|
pubmed:articleTitle |
Crystal structure of the HhaI DNA methyltransferase complexed with S-adenosyl-L-methionine.
|
pubmed:affiliation |
W. M. Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, New York 11724.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
|