PMID:8857533

Citation	Kamada, K, Horiuchi, T, Ohsumi, K, Shimamoto, N and Morikawa, K (1996) Structure of a replication-terminator protein complexed with DNA. Nature 383:598-603
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.
Links	PubMed Online version:10.1038/383598a0
Keywords	Amino Acid Sequence; Bacillus subtilis/chemistry; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Crystallography, X-Ray; DNA Replication; DNA, Bacterial/biosynthesis; DNA, Bacterial/chemistry; DNA, Bacterial/metabolism; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/metabolism; Escherichia coli/chemistry; Escherichia coli Proteins; Models, Molecular; Molecular Sequence Data; Mutation; Nucleic Acid Conformation; Protein Binding; Protein Conformation
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.