1ecr: Difference between revisions

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[[Image:1ecr.gif|left|200px]]
{{Seed}}
[[Image:1ecr.png|left|200px]]


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{{STRUCTURE_1ecr|  PDB=1ecr  |  SCENE=  }}  
{{STRUCTURE_1ecr|  PDB=1ecr  |  SCENE=  }}  


'''ESCHERICHIA COLI REPLICATION TERMINATOR PROTEIN (TUS) COMPLEXED WITH DNA'''
===ESCHERICHIA COLI REPLICATION TERMINATOR PROTEIN (TUS) COMPLEXED WITH DNA===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_8857533}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 8857533 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8857533}}


==About this Structure==
==About this Structure==
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[[Category: Dna replication]]
[[Category: Dna replication]]
[[Category: Dna-binding]]
[[Category: Dna-binding]]
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