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1ECR

ESCHERICHIA COLI REPLICATION TERMINATOR PROTEIN (TUS) COMPLEXED WITH DNA

Summary for 1ECR
Entry DOI10.2210/pdb1ecr/pdb
DescriptorDNA (5'-D(*TP*TP*AP*GP*TP*TP*AP*CP*AP*AP*CP*AP*TP*AP*CP*T)-3, DNA (5'-D(*TP*AP*GP*TP*AP*TP*GP*TP*TP*GP*TP*AP*AP*CP*TP*A)-3, PROTEIN (REPLICATION-TERMINATOR PROTEIN), ... (4 entities in total)
Functional Keywordsdna-binding, dna replication, complex (dna-binding protein-dna), replication-dna complex, replication/dna
Biological sourceEscherichia coli
Total number of polymer chains3
Total formula weight45626.60
Authors
Kamada, K.,Morikawa, K. (deposition date: 1996-09-01, release date: 1997-09-05, Last modification date: 2024-02-07)
Primary citationKamada, K.,Horiuchi, T.,Ohsumi, K.,Shimamoto, N.,Morikawa, K.
Structure of a replication-terminator protein complexed with DNA.
Nature, 383:598-603, 1996
Cited by
PubMed 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.
PubMed: 8857533
DOI: 10.1038/383598a0
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

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