Structural highlights
Function
[TUS_ECOLI] Trans-acting protein required for termination of DNA replication. Binds to DNA replication terminator sequences (terA to terF) to prevent the passage of replication forks. The termination efficiency will be affected by the affinity of this protein for the terminator sequence.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of a replication-terminator protein complexed with DNA.,Kamada K, Horiuchi T, Ohsumi K, Shimamoto N, Morikawa K Nature. 1996 Oct 17;383(6601):598-603. PMID:8857533[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kamada K, Horiuchi T, Ohsumi K, Shimamoto N, Morikawa K. Structure of a replication-terminator protein complexed with DNA. Nature. 1996 Oct 17;383(6601):598-603. PMID:8857533 doi:http://dx.doi.org/10.1038/383598a0
