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1ecr
From Proteopedia
| 1ecr, resolution 2.70Å () | |||||||||
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| Domains: | Ter | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
ESCHERICHIA COLI REPLICATION TERMINATOR PROTEIN (TUS) COMPLEXED WITH DNA
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1ECR is a 3 chains structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
- 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:10.1038/383598a0
Page seeded by OCA on Tue Feb 17 09:23:33 2009
