|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
4
|
|
pubmed:dateCreated |
1997-3-17
|
|
pubmed:abstractText |
The 552 amino acid vaccinia virus DNA ligase consists of three structural domains defined by partial proteolysis: (i) an amino-terminal 175 amino acid segment that is susceptible to digestion with chymotrypsin and trypsin; (ii) a protease-resistant central domain that contains the active site of nucleotidyl transfer (Lys-231); (iii) a protease-resistant carboxyl domain. The two protease-resistant domains are separated by a protease-sensitive interdomain bridge from positions 296 to 307. Adenylyltransferase and DNA ligation activities are preserved when the N-terminal 200 amino acids are deleted. However, the truncated form of vaccinia ligase has a reduced catalytic rate in strand joining and a lower affinity for DNA than does the full-sized enzyme. The 350 amino acid catalytic core of the vaccinia ligase is similar in size and protease-sensitivity to the full-length bacteriophage T7 DNA ligase.
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016621-1437556,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016621-1445910,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016621-1497311,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016621-1756739,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016621-1956768,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016621-2204063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016621-2555782,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016621-4377758,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016621-4915295,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016621-7489727,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016621-7565692,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016621-7565775,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016621-7645238,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016621-7721901,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016621-7760816,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016621-7991582,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016621-8183907,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016621-8385101,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016621-8519771,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016621-8559059,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016621-8653795,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016621-8661420,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016621-8710497
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Feb
|
|
pubmed:issn |
0305-1048
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
15
|
|
pubmed:volume |
25
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
727-34
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:9016621-Adenosine Triphosphate,
pubmed-meshheading:9016621-Amino Acid Sequence,
pubmed-meshheading:9016621-DNA, Viral,
pubmed-meshheading:9016621-DNA Ligases,
pubmed-meshheading:9016621-Endopeptidases,
pubmed-meshheading:9016621-Hydrolysis,
pubmed-meshheading:9016621-Kinetics,
pubmed-meshheading:9016621-Molecular Sequence Data,
pubmed-meshheading:9016621-Nucleotidyltransferases,
pubmed-meshheading:9016621-Protein Binding,
pubmed-meshheading:9016621-Protein Structure, Tertiary,
pubmed-meshheading:9016621-Recombinant Proteins,
pubmed-meshheading:9016621-Sequence Deletion,
pubmed-meshheading:9016621-Vaccinia virus
|
|
pubmed:year |
1997
|
|
pubmed:articleTitle |
Domain structure of vaccinia DNA ligase.
|
|
pubmed:affiliation |
Molecular Biology Program, Sloan-Kettering Institute, New York 10021, USA.
|
|
pubmed:publicationType |
Journal Article
|
