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E. coli DNA topoisomerases.
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创建时间:
2019-12-12
相关数据集
HUMAN DNA TOPOISOMERASE I IN COVALENT COMPLEX WITH A 22 BASE PAIR DNA DUPLEX
HUMAN DNA TOPOISOMERASE I IN COVALENT COMPLEX WITH A 22 BASE PAIR DNA DUPLEX Descriptor: 5'-D(*(SPT)P*GP*AP*AP*AP*AP*AP*(5IU)P*(5IU)P*(5IU)P*(5IU)P*T)-3', 5'-D(*AP*AP*AP*AP*AP*GP*AP*CP*(5IU)P*(5IU))-3
Protein Data Bank Japan2024-11-06 更新50
Flow Magnetic Tweezers: Gyrase dynamics under 3 different external torque conditions. Part 2/3
The video contains a whole field from a force spectroscopy experiment called Flow Magnetic Tweezers (FMT). It shows E. coli DNA Gyrase manipulating DNA topology by relaxing positive and introducing ne
NIAID Data Ecosystem50
Structural similarities between topoisomerases that cleave one or both DNA strands
Type IA and type II DNA topoisomerases are distinguished by their ability to cleave one or two strands, respectively, of a DNA duplex. Both types have been proposed to use an “enzyme-bridging” mechani
PubMed Central1998-07-07 更新20
Crystal structure of dna gyrase B' domain sheds lights on the mechanism for T-segment navigation
Crystal structure of dna gyrase B' domain sheds lights on the mechanism for T-segment navigation Descriptor: DNA gyrase subunit B Authors: Fu, G.S, Zhu, D.Y, Hu, Y.L, Wang, D.C. Deposit date: 2008-03-
Protein Data Bank Japan2024-03-13 更新50
Table_2_Single-nucleotide resolution detection of Topo IV cleavage activity in the Escherichia coli genome with Topo-Seq.xlsx
Topoisomerase IV (Topo IV) is the main decatenation enzyme in Escherichia coli; it removes catenation links that are formed during DNA replication. Topo IV binding and cleavage sites were previously i
NIAID Data Ecosystem20



