Structure/function correlations in Pseudomonas aeruginosa DNA ligase LigD
Item
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Title
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Structure/function correlations in Pseudomonas aeruginosa DNA ligase LigD
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Identifier
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d_2009_2013:4f3956493f99:10772
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identifier
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11064
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Creator
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Natarajan, Aswin,
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Contributor
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Ranajeet Ghose
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Date
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2011
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Language
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English
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Publisher
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City University of New York.
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Subject
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Biochemistry | Biophysics | DNA ligase | LigD | NHEJ | Phosphoesterase
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Abstract
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The ATP-dependent DNA ligase D (LigD) performs a major role in the non-homologous end-joining (NHEJ) pathway. Pseudomonas aeruginosa LigD contains a N-terminal phosphoesterase domain (PE) domain followed by a ligase domain and a C-terminal polymerase domain. The PE domain (187 residues), belonging to a class of unique 3'-end-processing enzymes, possesses manganese dependent phosphodiesterase and phosphomonoesterase activities as it sequentially removes the 3'-ribonucleoside from the primer strand of the primer-template DNA duplex and hydrolyzes the 3'-PO4 produced finally to a 3'-OH group. Extensive mutagenesis and biochemical studies have identified critical residues and important features required for 3'-ribonuclease and 3'-- phosphatase activities. Lack of sequence homology to other known nucleases lead to the belief that this enzyme possesses some unique motifs. However, in the absence of atomic level structural information clear structure/function correlations were lacking. This thesis describes the procedures used to obtain a high-resolution structure of PE domain obtained using solution NMR methods and to ascertain its interaction with DNA substrates.
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Type
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dissertation
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Source
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2009_2013.csv
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degree
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Ph.D.
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Program
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Biochemistry
