Nucleic Acids Research, Vol 25, Issue 4 727-734, Copyright © 1997 by Oxford University Press
J Sekiguchi and S Shuman
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.
ARTICLES
Domain structure of vaccinia DNA ligase
Molecular Biology Program, Sloan-Kettering Institute, New York 10021, USA.
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