Structure of a replication-terminator protein complexed with DNA - PubMed (original) (raw)

. 1996 Oct 17;383(6601):598-603.

doi: 10.1038/383598a0.

Affiliations

• PMID: 8857533
• DOI: 10.1038/383598a0

Structure of a replication-terminator protein complexed with DNA

K Kamada et al. Nature. 1996.

Abstract

The crystal structure of the Escherichia coli replication-terminator protein (Tus) bound to terminus-site (Ter) DNA has been determined at 2.7 A 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 beta-strands. The unusual structural features of this complex may explain how the replication fork is halted in only one direction.

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Comment in

• DNA replication. Tussle with a terminator.
  Wake RG. Wake RG. Nature. 1996 Oct 17;383(6601):582-3. doi: 10.1038/383582a0. Nature. 1996. PMID: 8857531 No abstract available.

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