5noc
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='5noc' size='340' side='right' caption='[[5noc]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='5noc' size='340' side='right' caption='[[5noc]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5noc]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NOC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NOC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5noc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NOC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NOC FirstGlance]. <br> |
| - | </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=5noc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5noc OCA], [http://pdbe.org/5noc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5noc RCSB], [http://www.ebi.ac.uk/pdbsum/5noc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5noc ProSAT]</span></td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spo0J, BSU40960 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</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=5noc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5noc OCA], [http://pdbe.org/5noc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5noc RCSB], [http://www.ebi.ac.uk/pdbsum/5noc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5noc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/SP0J_BACSU SP0J_BACSU]] Required for the initiation of sporulation and for normal chromosome segregation. Antagonizes sporulation inhibition by Soj. It probably interacts with a specific DNA site and other proteins involved in partitioning and cell division, and antagonizes Soj in response to cell cycle events related to chromosome partitioning.<ref>PMID:8071208</ref> | [[http://www.uniprot.org/uniprot/SP0J_BACSU SP0J_BACSU]] Required for the initiation of sporulation and for normal chromosome segregation. Antagonizes sporulation inhibition by Soj. It probably interacts with a specific DNA site and other proteins involved in partitioning and cell division, and antagonizes Soj in response to cell cycle events related to chromosome partitioning.<ref>PMID:8071208</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The ParB protein forms DNA bridging interactions around parS to condense DNA and earmark the bacterial chromosome for segregation. The molecular mechanism underlying the formation of these ParB networks is unclear. We show here that while the central DNA binding domain is essential for anchoring at parS, this interaction is not required for DNA condensation. Structural analysis of the C-terminal domain reveals a dimer with a lysine-rich surface that binds DNA non-specifically and is essential for DNA condensation in vitro. Mutation of either the dimerisation or the DNA binding interface eliminates ParB-GFP foci formation in vivo. Moreover, the free C-terminal domain can rapidly decondense ParB networks independently of its ability to bind DNA. Our work reveals a dual role for the C-terminal domain of ParB as both a DNA binding and bridging interface, and highlights the dynamic nature of ParB networks in Bacillus subtilis. | ||
| + | |||
| + | The structural basis for dynamic DNA binding and bridging interactions which condense the bacterial centromere.,Fisher GL, Pastrana CL, Higman VA, Koh A, Taylor JA, Butterer A, Craggs T, Sobott F, Murray H, Crump MP, Moreno-Herrero F, Dillingham MS Elife. 2017 Dec 15;6. doi: 10.7554/eLife.28086. PMID:29244022<ref>PMID:29244022</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5noc" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bacsu]] | ||
[[Category: Crump, M P]] | [[Category: Crump, M P]] | ||
[[Category: Dillingham, M S]] | [[Category: Dillingham, M S]] | ||
Revision as of 08:51, 27 December 2017
Solution NMR Structure of the C-terminal domain of ParB (Spo0J)
| |||||||||||
