1f4k

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f4k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f4k RCSB], [http://www.ebi.ac.uk/pdbsum/1f4k PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f4k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f4k RCSB], [http://www.ebi.ac.uk/pdbsum/1f4k PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/RTP_BACSU RTP_BACSU]] Plays a role in DNA replication and termination (fork arrest mechanism). Two dimers of rtp bind to the two inverted repeat regions (IRI and IRII) present in the termination site. The binding of each dimer is centered on an 8 bp direct repeat.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 17:58, 24 December 2014

CRYSTAL STRUCTURE OF THE REPLICATION TERMINATOR PROTEIN/B-SITE DNA COMPLEX

1f4k, resolution 2.50Å

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