Structure of a replication-terminator protein complexed with DNA

Abstract

The crystal structure of the Escherichia colireplication-terminator protein (Tus) bound to terminus-site (Ter) DNA has been determined at 2.7 Å resolution. The Tus protein folds into a previously undescribed architecture divided into two domains by a central basic cleft. This cleft accommodates locally deformed B-form Ter DNA and makes extensive contacts with the major groove, mainly through two interdomain β-strands. The unusual structural features of this complex may explain how the replication fork is halted in only one direction.

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