Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2002-11-19
pubmed:abstractText
Escherichia coli DNA topoisomerase I binds three Zn(II) with three tetracysteine motifs which, together with the 14 kDa C-terminal region, form a 30 kDa DNA binding domain (ZD domain). The 67 kDa N-terminal domain (Top67) has the active site tyrosine for DNA cleavage but cannot relax negatively supercoiled DNA. We analyzed the role of the ZD domain in the enzyme mechanism.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-10347234, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-10419478, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-10502515, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-10504717, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-10574789, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-10636841, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-10692165, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-10734115, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-10873443, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-11395412, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-11577108, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-12844870, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-12844883, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-1313943, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-1650356, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-1846973, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-2108957, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-227859, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-2560191, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-2843517, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-2846526, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-3029380, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-338610, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-4279300, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-6099250, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-6155377, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-6253080, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-6265907, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-6277910, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-6305585, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-6326814, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-7510701, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-7623379, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-7798272, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-7826860, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-8114910, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-8300610, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-8396651, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-8621552, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-9497321, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-9524255, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-9593741, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-9748482, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-9769215, http://linkedlifedata.com/resource/pubmed/commentcorrection/12052259-9792804
pubmed:language
eng
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:author
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13
pubmed:dateRevised
2010-11-18
pubmed:articleTitle
The role of the Zn(II) binding domain in the mechanism of E. coli DNA topoisomerase I.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, New York Medical College, Valhalla, NY, USA. a_ahumada@msn.com