|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5oqr' size='340' side='right'caption='[[5oqr]], [[Resolution|resolution]] 2.61Å' scene=''> | | <StructureSection load='5oqr' size='340' side='right'caption='[[5oqr]], [[Resolution|resolution]] 2.61Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5oqr]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OQR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5OQR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5oqr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OQR FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5oqn|5oqn]], [[5oqo|5oqo]], [[5oqp|5oqp]], [[5oqq|5oqq]]</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]] 2.61Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5oqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oqr OCA], [http://pdbe.org/5oqr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oqr RCSB], [http://www.ebi.ac.uk/pdbsum/5oqr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oqr 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=5oqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oqr OCA], [https://pdbe.org/5oqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oqr RCSB], [https://www.ebi.ac.uk/pdbsum/5oqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oqr ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CND3_SCHPO CND3_SCHPO]] Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. The condensin complex probably also plays a role during interphase.<ref>PMID:10485849</ref> [[http://www.uniprot.org/uniprot/CND2_SCHPO CND2_SCHPO]] Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. The condensin complex probably also plays a role during interphase in processes such as DNA repair.<ref>PMID:10485849</ref> <ref>PMID:12000964</ref> | + | [https://www.uniprot.org/uniprot/CND3_SCHPO CND3_SCHPO] Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. The condensin complex probably also plays a role during interphase.<ref>PMID:10485849</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 26: |
Line 26: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Haering, C H]] | + | [[Category: Schizosaccharomyces pombe 972h-]] |
| - | [[Category: Hassler, M]] | + | [[Category: Haering CH]] |
| - | [[Category: Kschonsak, M]] | + | [[Category: Hassler M]] |
| - | [[Category: Cell cycle]] | + | [[Category: Kschonsak M]] |
| - | [[Category: Dna-binding]]
| + | |
| - | [[Category: Heat repeat]]
| + | |
| - | [[Category: Kleisin]]
| + | |
| - | [[Category: Smc complex]]
| + | |
| Structural highlights
Function
CND3_SCHPO Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. The condensin complex probably also plays a role during interphase.[1]
Publication Abstract from PubMed
Condensin protein complexes coordinate the formation of mitotic chromosomes and thereby ensure the successful segregation of replicated genomes. Insights into how condensin complexes bind to chromosomes and alter their topology are essential for understanding the molecular principles behind the large-scale chromatin rearrangements that take place during cell divisions. Here, we identify a direct DNA-binding site in the eukaryotic condensin complex, which is formed by its Ycg1Cnd3 HEAT-repeat and Brn1Cnd2 kleisin subunits. DNA co-crystal structures reveal a conserved, positively charged groove that accommodates the DNA double helix. A peptide loop of the kleisin subunit encircles the bound DNA and, like a safety belt, prevents its dissociation. Firm closure of the kleisin loop around DNA is essential for the association of condensin complexes with chromosomes and their DNA-stimulated ATPase activity. Our data suggest a sophisticated molecular basis for anchoring condensin complexes to chromosomes that enables the formation of large-sized chromatin loops.
Structural Basis for a Safety-Belt Mechanism That Anchors Condensin to Chromosomes.,Kschonsak M, Merkel F, Bisht S, Metz J, Rybin V, Hassler M, Haering CH Cell. 2017 Oct 4. pii: S0092-8674(17)31057-7. doi: 10.1016/j.cell.2017.09.008. PMID:28988770[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sutani T, Yuasa T, Tomonaga T, Dohmae N, Takio K, Yanagida M. Fission yeast condensin complex: essential roles of non-SMC subunits for condensation and Cdc2 phosphorylation of Cut3/SMC4. Genes Dev. 1999 Sep 1;13(17):2271-83. PMID:10485849
- ↑ Kschonsak M, Merkel F, Bisht S, Metz J, Rybin V, Hassler M, Haering CH. Structural Basis for a Safety-Belt Mechanism That Anchors Condensin to Chromosomes. Cell. 2017 Oct 4. pii: S0092-8674(17)31057-7. doi: 10.1016/j.cell.2017.09.008. PMID:28988770 doi:http://dx.doi.org/10.1016/j.cell.2017.09.008
|
