Nucleic Acids Research, Vol 25, Issue 21 4224-4229, Copyright © 1997 by Oxford University Press
PJ Artymiuk, TA Ceska, D Suck and JR Sayers
The three dimensional crystal structure of T5 5'-3' exonuclease was
compared with that of two other members of the 5'-3' exonuclease family: T4
ribonuclease H and the N-terminal domain of Thermus aquaticus DNA
polymerase I. Though these structures were largely similar, some regions of
these enzymes show evidence of significant molecular flexibility. Previous
sequence analysis had suggested the existence of a helix-hairpin-helix
motif in T5 exonuclease, but a distinct, though related structure is
actually found to occur. The entire T5 exonuclease structure was then
compared with all the structures in the complete Protein Data Bank and an
unexpected similarity with gamma-delta (gamma delta) resolvase was
observed. 5'-3' exonucleases and gamma delta resolvase are enzymes involved
in carrying out quite different manipulations on nucleic acids. They appear
to be unrelated at the primary sequence level, yet the fold of the entire
catalytic domain of gamma delta resolvase is contained within that of the
5'-3'exonuclease. Different large-scale helical structures are used by both
families to form DNA binding sites.
ARTICLES
Prokaryotic 5'-3' exonucleases share a common core structure with gamma- delta resolvase
Department of Molecular Biology and Biotechnology and Department of Molecular and Genetic Medicine, Krebs Institute, The University of Sheffield, Sheffield S10 2JF, UK.
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