2efw

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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=2efw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2efw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2efw RCSB], [http://www.ebi.ac.uk/pdbsum/2efw 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=2efw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2efw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2efw RCSB], [http://www.ebi.ac.uk/pdbsum/2efw 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 17:05, 25 December 2014

Crystal structure of the RTP:nRB complex from Bacillus subtilis

2efw, resolution 2.50Å

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