1ecr: Difference between revisions

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[[Image:1ecr.gif|left|200px]]
[[Image:1ecr.gif|left|200px]]


{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ecr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ecr OCA], [http://www.ebi.ac.uk/pdbsum/1ecr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ecr RCSB]</span>
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'''ESCHERICHIA COLI REPLICATION TERMINATOR PROTEIN (TUS) COMPLEXED WITH DNA'''
'''ESCHERICHIA COLI REPLICATION TERMINATOR PROTEIN (TUS) COMPLEXED WITH DNA'''
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[[Category: Kamada, K.]]
[[Category: Kamada, K.]]
[[Category: Morikawa, K.]]
[[Category: Morikawa, K.]]
[[Category: complex (dna-binding protein/dna)]]
[[Category: Dna replication]]
[[Category: dna replication]]
[[Category: Dna-binding]]
[[Category: dna-binding]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:56:29 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:59:58 2008''

Revision as of 14:56, 2 May 2008

File:1ecr.gif


PDB ID 1ecr

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1ecr, resolution 2.70Å ()
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



ESCHERICHIA COLI REPLICATION TERMINATOR PROTEIN (TUS) COMPLEXED WITH DNA


OverviewOverview

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.

About this StructureAbout this Structure

1ECR is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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 Page seeded by OCA on Fri May 2 14:56:29 2008

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