1bm9: Difference between revisions

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<StructureSection load='1bm9' size='340' side='right'caption='[[1bm9]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1bm9' size='340' side='right'caption='[[1bm9]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1bm9]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BM9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BM9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1bm9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BM9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BM9 FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bm9 OCA], [https://pdbe.org/1bm9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bm9 RCSB], [https://www.ebi.ac.uk/pdbsum/1bm9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bm9 ProSAT]</span></td></tr>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bm9 OCA], [https://pdbe.org/1bm9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bm9 RCSB], [https://www.ebi.ac.uk/pdbsum/1bm9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bm9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://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.  
[https://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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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bastia, D]]
[[Category: Bastia D]]
[[Category: Bussiere, D E]]
[[Category: Bussiere DE]]
[[Category: White, S]]
[[Category: White S]]
[[Category: Contrahelicase]]
[[Category: Dna-binding protein]]

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