3veb
From Proteopedia
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| - | [[ | + | ==Crystal Structure of Matp-matS== |
| + | <StructureSection load='3veb' size='340' side='right' caption='[[3veb]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3veb]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VEB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VEB FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vea|3vea]], [[4d8j|4d8j]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">matP, YPO1433, y2737, YP_0877 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=632 Yersinia pestis])</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=3veb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3veb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3veb RCSB], [http://www.ebi.ac.uk/pdbsum/3veb PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The E. coli chromosome is condensed into insulated regions termed macrodomains (MDs), which are essential for genomic packaging. How chromosomal MDs are specifically organized and compacted is unknown. Here, we report studies revealing the molecular basis for Terminus-containing (Ter) chromosome condensation by the Ter-specific factor MatP. MatP contains a tripartite fold with a four-helix bundle DNA-binding motif, ribbon-helix-helix and C-terminal coiled-coil. Strikingly, MatP-matS structures show that the MatP coiled-coils form bridged tetramers that flexibly link distant matS sites. Atomic force microscopy and electron microscopy studies demonstrate that MatP alone loops DNA. Mutation of key coiled-coil residues destroys looping and causes a loss of Ter condensation in vivo. Thus, these data reveal the molecular basis for a protein-mediated DNA-bridging mechanism that mediates condensation of a large chromosomal domain in enterobacteria. | ||
| - | + | Molecular Basis for a Protein-Mediated DNA-Bridging Mechanism that Functions in Condensation of the E. coli Chromosome.,Dupaigne P, Tonthat NK, Espeli O, Whitfill T, Boccard F, Schumacher MA Mol Cell. 2012 Oct 16. pii: S1097-2765(12)00785-X. doi:, 10.1016/j.molcel.2012.09.009. PMID:23084832<ref>PMID:23084832</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Yersinia pestis]] | [[Category: Yersinia pestis]] | ||
| - | [[Category: Schumacher, M A | + | [[Category: Schumacher, M A]] |
[[Category: Chromosome]] | [[Category: Chromosome]] | ||
[[Category: Dna binding protein-dna complex]] | [[Category: Dna binding protein-dna complex]] | ||
[[Category: Dna condensation]] | [[Category: Dna condensation]] | ||
[[Category: Macrodomain]] | [[Category: Macrodomain]] | ||
Revision as of 17:21, 9 December 2014
Crystal Structure of Matp-matS
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