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Sequence-specific 1HN, 13C, and 15N backbone resonance assignments of the 34kDa Paramecium bursaria Chlorella virus 1 (PBCV1) DNA ligase

Sequence-specific 1HN, 13C, and 15N backbone resonance assignments of the 34kDa Paramecium... Chlorella virus DNA ligase (ChVLig) is a minimal (298-amino acid) pluripotent ATP-dependent ligase composed of three structural modules—a nucleotidyltransferase domain, an OB domain, and a β-hairpin latch—that forms a circumferential clamp around nicked DNA. ChVLig provides an instructive model to understand the chemical and conformational steps of nick repair. Here we report the assignment of backbone 13C, 15N, 1HN resonances of this 34.2 kDa protein, the first for a DNA ligase in full-length form. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biomolecular NMR Assignments Springer Journals

Sequence-specific 1HN, 13C, and 15N backbone resonance assignments of the 34kDa Paramecium bursaria Chlorella virus 1 (PBCV1) DNA ligase

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References (9)

Publisher
Springer Journals
Copyright
Copyright © 2009 by Springer Science+Business Media B.V.
Subject
Physics; Biological and Medical Physics, Biophysics; Polymer Sciences; Biochemistry, general
ISSN
1874-2718
eISSN
1874-270X
DOI
10.1007/s12104-009-9145-9
pmid
19636951
Publisher site
See Article on Publisher Site

Abstract

Chlorella virus DNA ligase (ChVLig) is a minimal (298-amino acid) pluripotent ATP-dependent ligase composed of three structural modules—a nucleotidyltransferase domain, an OB domain, and a β-hairpin latch—that forms a circumferential clamp around nicked DNA. ChVLig provides an instructive model to understand the chemical and conformational steps of nick repair. Here we report the assignment of backbone 13C, 15N, 1HN resonances of this 34.2 kDa protein, the first for a DNA ligase in full-length form.

Journal

Biomolecular NMR AssignmentsSpringer Journals

Published: Jan 13, 2009

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