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| | ==Crystal structure of the complex between ScpA(residues 1-160)-ScpB(residues 1-183)== | | ==Crystal structure of the complex between ScpA(residues 1-160)-ScpB(residues 1-183)== |
| - | <StructureSection load='4i98' size='340' side='right' caption='[[4i98]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='4i98' size='340' side='right'caption='[[4i98]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4i98]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Strzp Strzp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I98 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I98 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4i98]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_P1031 Streptococcus pneumoniae P1031]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I98 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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4i99|4i99]]</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=4i98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i98 OCA], [https://pdbe.org/4i98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i98 RCSB], [https://www.ebi.ac.uk/pdbsum/4i98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i98 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">scpA, SPP_1876 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=488223 STRZP]), scpB, SPP_1875 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=488223 STRZP])</td></tr>
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| - | <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=4i98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i98 OCA], [http://pdbe.org/4i98 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4i98 RCSB], [http://www.ebi.ac.uk/pdbsum/4i98 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4i98 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SCPA_STRZP SCPA_STRZP]] Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves (By similarity). [[http://www.uniprot.org/uniprot/SCPB_STRZP SCPB_STRZP]] Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpA that pull DNA away from mid-cell into both cell halves (By similarity). | + | [https://www.uniprot.org/uniprot/SCPA_STRZP SCPA_STRZP] Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Strzp]] | + | [[Category: Large Structures]] |
| - | [[Category: Oh, B H]] | + | [[Category: Streptococcus pneumoniae P1031]] |
| - | [[Category: Shin, H C]] | + | [[Category: Oh BH]] |
| - | [[Category: Cell cycle]] | + | [[Category: Shin HC]] |
| - | [[Category: Dna condensation]]
| + | |
| - | [[Category: Scpa]]
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| - | [[Category: Scpb]]
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| - | [[Category: Smc]]
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| Structural highlights
Function
SCPA_STRZP Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves (By similarity).
Publication Abstract from PubMed
Eukaryotic structural maintenance of chromosomes (SMC)-kleisin complexes form large, ring-shaped assemblies that promote accurate chromosome segregation. Their asymmetric structural core comprises SMC heterodimers that associate with both ends of a kleisin subunit. However, prokaryotic condensin Smc-ScpAB is composed of symmetric Smc homodimers associated with the kleisin ScpA in a postulated symmetrical manner. Here, we demonstrate that Smc molecules have two distinct binding sites for ScpA. The N terminus of ScpA binds the Smc coiled coil, whereas the C terminus binds the Smc ATPase domain. We show that in Bacillus subtilis cells, an Smc dimer is bridged by a single ScpAB to generate asymmetric tripartite rings analogous to eukaryotic SMC complexes. We define a molecular mechanism that ensures asymmetric assembly, and we conclude that the basic architecture of SMC-kleisin rings evolved before the emergence of eukaryotes.
An asymmetric SMC-kleisin bridge in prokaryotic condensin.,Burmann F, Shin HC, Basquin J, Soh YM, Gimenez-Oya V, Kim YG, Oh BH, Gruber S Nat Struct Mol Biol. 2013 Jan 27;20(3):371-9. doi: 10.1038/nsmb.2488. Epub 2013, Jan 27. PMID:23353789[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Burmann F, Shin HC, Basquin J, Soh YM, Gimenez-Oya V, Kim YG, Oh BH, Gruber S. An asymmetric SMC-kleisin bridge in prokaryotic condensin. Nat Struct Mol Biol. 2013 Jan 27;20(3):371-9. doi: 10.1038/nsmb.2488. Epub 2013, Jan 27. PMID:23353789 doi:http://dx.doi.org/10.1038/nsmb.2488
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