View source for 4i98


==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]] 2.80&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</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'>[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>
</table>
== Function ==
[https://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).
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4i98" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus pneumoniae P1031]]
[[Category: Oh BH]]
[[Category: Shin HC]]