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4i98

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[[Image:4i98.jpg|left|200px]]
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==Crystal structure of the complex between ScpA(residues 1-160)-ScpB(residues 1-183)==
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<StructureSection load='4i98' size='340' side='right' caption='[[4i98]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4i99|4i99]]</td></tr>
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<tr><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><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://www.rcsb.org/pdb/explore.do?structureId=4i98 RCSB], [http://www.ebi.ac.uk/pdbsum/4i98 PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_4i98| PDB=4i98 | SCENE= }}
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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>
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===Crystal structure of the complex between ScpA(residues 1-160)-ScpB(residues 1-183)===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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==About this Structure==
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<references/>
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[[4i98]] is a 3 chain structure with sequence from [http://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].
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__TOC__
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[[Category: Streptococcus pneumoniae p1031]]
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</StructureSection>
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[[Category: Oh, B.]]
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[[Category: Strzp]]
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[[Category: Shin, H.]]
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[[Category: Oh, B H.]]
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[[Category: Shin, H C.]]
[[Category: Cell cycle]]
[[Category: Cell cycle]]
[[Category: Dna condensation]]
[[Category: Dna condensation]]

Revision as of 07:13, 10 September 2014

Crystal structure of the complex between ScpA(residues 1-160)-ScpB(residues 1-183)

4i98, resolution 2.80Å

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