3vea

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Current revision (14:26, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3vea' size='340' side='right'caption='[[3vea]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
<StructureSection load='3vea' size='340' side='right'caption='[[3vea]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3vea]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_pestis"_(lehmann_and_neumann_1896)_migula_1900 "bacillus pestis" (lehmann and neumann 1896) migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VEA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3vea]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VEA FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3veb|3veb]], [[4d8j|4d8j]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">matP, y2737, YPO1433, YP_0877 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=632 "Bacillus pestis" (Lehmann and Neumann 1896) Migula 1900])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vea OCA], [https://pdbe.org/3vea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vea RCSB], [https://www.ebi.ac.uk/pdbsum/3vea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vea ProSAT]</span></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=3vea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vea OCA], [https://pdbe.org/3vea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vea RCSB], [https://www.ebi.ac.uk/pdbsum/3vea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vea ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/MATP_YERPE MATP_YERPE]] Required for spatial organization of the terminus region of the chromosome (Ter macrodomain) during the cell cycle. Prevents early segregation of duplicated Ter macrodomains during cell division. Binds specifically to matS, which is a 13 bp signature motif repeated within the Ter macrodomain.[HAMAP-Rule:MF_01073]
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[https://www.uniprot.org/uniprot/MATP_YERPE MATP_YERPE] Required for spatial organization of the terminus region of the chromosome (Ter macrodomain) during the cell cycle. Prevents early segregation of duplicated Ter macrodomains during cell division. Binds specifically to matS, which is a 13 bp signature motif repeated within the Ter macrodomain.[HAMAP-Rule:MF_01073]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3vea" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Schumacher, M A]]
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[[Category: Yersinia pestis]]
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[[Category: Chromosome]]
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[[Category: Schumacher MA]]
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[[Category: Dna binding protein-dna complex]]
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[[Category: Dna condensation]]
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[[Category: Macrodomain]]
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Current revision

Crystal Structure of matP-matS23mer

PDB ID 3vea

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