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6h2x

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Revision as of 07:34, 1 May 2024

MukB coiled-coil elbow from E. coli

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OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6h2x"

Categories: Escherichia coli K-12 | Large Structures | Buermann F | Lowe J

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 <StructureSection load='6h2x' size='340' side='right'caption='[[6h2x]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6h2x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H2X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H2X FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6h2x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6H2X FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mukB, b0924, JW0907 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=6h2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h2x OCA], [http://pdbe.org/6h2x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h2x RCSB], [http://www.ebi.ac.uk/pdbsum/6h2x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h2x 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=6h2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h2x OCA], [https://pdbe.org/6h2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6h2x RCSB], [https://www.ebi.ac.uk/pdbsum/6h2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6h2x ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MUKB_ECOLI MUKB_ECOLI]] Plays a central role in chromosome condensation, segregation and cell cycle progression. Functions as a homodimer, which is essential for chromosome partition. Involved in negative DNA supercoiling in vivo, and by this means organizes and compacts chromosomes. May achieve or facilitate chromosome segregation by condensation of DNA from both sides of a centrally located replisome during cell division. Stimulates both DNA relaxation and to a lesser extent decatenation activity of topoisomerase IV.<ref>PMID:20921377</ref> <ref>PMID:10660686</ref>
+[https://www.uniprot.org/uniprot/MUKB_ECOLI MUKB_ECOLI] Plays a central role in chromosome condensation, segregation and cell cycle progression. Functions as a homodimer, which is essential for chromosome partition. Involved in negative DNA supercoiling in vivo, and by this means organizes and compacts chromosomes. May achieve or facilitate chromosome segregation by condensation of DNA from both sides of a centrally located replisome during cell division. Stimulates both DNA relaxation and to a lesser extent decatenation activity of topoisomerase IV.<ref>PMID:20921377</ref> <ref>PMID:10660686</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Structural maintenance of chromosomes (SMC)-kleisin complexes organize chromosomal DNAs in all domains of life, with key roles in chromosome segregation, DNA repair and regulation of gene expression. They function through the entrapment and active translocation of DNA, but the underlying conformational changes are largely unclear. Using structural biology, mass spectrometry and cross-linking, we investigated the architecture of two evolutionarily distant SMC-kleisin complexes: MukBEF from Escherichia coli, and cohesin from Saccharomyces cerevisiae. We show that both contain a dynamic coiled-coil discontinuity, the elbow, near the middle of their arms that permits a folded conformation. Bending at the elbow brings into proximity the hinge dimerization domain and the head-kleisin module, situated at opposite ends of the arms. Our findings favour SMC activity models that include a large conformational change in the arms, such as a relative movement between DNA contact sites during DNA loading and translocation.
-A folded conformation of MukBEF and cohesin.,Burmann F, Lee BG, Than T, Sinn L, O'Reilly FJ, Yatskevich S, Rappsilber J, Hu B, Nasmyth K, Lowe J Nat Struct Mol Biol. 2019 Mar;26(3):227-236. doi: 10.1038/s41594-019-0196-z. Epub, 2019 Mar 4. PMID:30833788<ref>PMID:30833788</ref>
+==See Also==
+*[[Condensin|Condensin]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 6h2x" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Ecoli]]
+[[Category: Escherichia coli K-12]]
 [[Category: Large Structures]]
-[[Category: Buermann, F]]
+[[Category: Buermann F]]
-[[Category: Lowe, J]]
+[[Category: Lowe J]]
-[[Category: Chromosome organization]]
-[[Category: Chromosome segregation]]
-[[Category: Coiled coil]]
-[[Category: Dna binding protein]]

6h2x

From Proteopedia

Revision as of 07:34, 1 May 2024

MukB coiled-coil elbow from E. coli

Structural highlights

Function

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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