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| <StructureSection load='6h2x' size='340' side='right'caption='[[6h2x]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='6h2x' size='340' side='right'caption='[[6h2x]], [[Resolution|resolution]] 2.60Å' scene=''> |
| == Structural highlights == | | == 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]] 2.6Å</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> | | </table> |
| == Function == | | == 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;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| </div> | | </div> |
| <div class="pdbe-citations 6h2x" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6h2x" style="background-color:#fffaf0;"></div> |
| + | |
| + | ==See Also== |
| + | *[[Condensin|Condensin]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| [[Category: Large Structures]] | | [[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]]
| + | |
| Structural highlights
Function
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.[1] [2]
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li Y, Stewart NK, Berger AJ, Vos S, Schoeffler AJ, Berger JM, Chait BT, Oakley MG. Escherichia coli condensin MukB stimulates topoisomerase IV activity by a direct physical interaction. Proc Natl Acad Sci U S A. 2010 Nov 2;107(44):18832-7. doi:, 10.1073/pnas.1008678107. Epub 2010 Oct 4. PMID:20921377 doi:http://dx.doi.org/10.1073/pnas.1008678107
- ↑ Sawitzke JA, Austin S. Suppression of chromosome segregation defects of Escherichia coli muk mutants by mutations in topoisomerase I. Proc Natl Acad Sci U S A. 2000 Feb 15;97(4):1671-6. PMID:10660686 doi:http://dx.doi.org/10.1073/pnas.030528397
- ↑ Burmann F, Lee BG, Than T, Sinn L, O'Reilly FJ, Yatskevich S, Rappsilber J, Hu B, Nasmyth K, Lowe J. A folded conformation of MukBEF and cohesin. Nat Struct Mol Biol. 2019 Mar;26(3):227-236. doi: 10.1038/s41594-019-0196-z. Epub, 2019 Mar 4. PMID:30833788 doi:http://dx.doi.org/10.1038/s41594-019-0196-z
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