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==Crystal structure of the kleisin-N SMC interface in prokaryotic condensin== | |||
<StructureSection load='3zgx' size='340' side='right'caption='[[3zgx]], [[Resolution|resolution]] 3.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3zgx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZGX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZGX FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4Å</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=3zgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zgx OCA], [https://pdbe.org/3zgx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zgx RCSB], [https://www.ebi.ac.uk/pdbsum/3zgx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zgx ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SMC_BACSU SMC_BACSU] Required for chromosome condensation and partitioning.<ref>PMID:9573042</ref> <ref>PMID:9701812</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:23353789</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3zgx" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[Condensin|Condensin]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Basquin | [[Category: Large Structures]] | ||
[[Category: Burmann | [[Category: Basquin J]] | ||
[[Category: Gimenez | [[Category: Burmann F]] | ||
[[Category: Gruber | [[Category: Gimenez V]] | ||
[[Category: Kim | [[Category: Gruber S]] | ||
[[Category: Oh | [[Category: Kim Y]] | ||
[[Category: Shin | [[Category: Oh B]] | ||
[[Category: Soh | [[Category: Shin H]] | ||
[[Category: Soh Y]] | |||
Latest revision as of 13:39, 9 May 2024
Crystal structure of the kleisin-N SMC interface in prokaryotic condensinCrystal structure of the kleisin-N SMC interface in prokaryotic condensin
Structural highlights
FunctionSMC_BACSU Required for chromosome condensation and partitioning.[1] [2] Publication Abstract from PubMedEukaryotic 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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