Domain structure of vaccinia DNA ligase.

Abstract

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.

• Authors: J Sekiguchi, S Shuman
• Journal: Nucleic acids research (Nucleic Acids Res) Vol. 25 Issue 4 Pg. 727-34 (Feb 15 1997) ISSN: 0305-1048 [Print] England
• PMID: 9016621 (Publication Type: Journal Article)

Chemical References

• DNA, Viral
• Recombinant Proteins
• Adenosine Triphosphate
• Nucleotidyltransferases
• Endopeptidases
• DNA Ligases

Topics

• Adenosine Triphosphate (physiology)
• Amino Acid Sequence
• DNA Ligases (chemistry, metabolism)
• DNA, Viral (metabolism)
• Endopeptidases
• Hydrolysis
• Kinetics
• Molecular Sequence Data
• Nucleotidyltransferases (chemistry)
• Protein Binding (genetics)
• Protein Structure, Tertiary
• Recombinant Proteins (metabolism)
• Sequence Deletion
• Vaccinia virus (enzymology)