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4i99

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'''Unreleased structure'''
 
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The entry 4i99 is ON HOLD
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==Crystal structure of the SmcHead bound to the C-winged helix domain of ScpA==
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<StructureSection load='4i99' size='340' side='right'caption='[[4i99]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4i99]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus_DSM_3638 Pyrococcus furiosus DSM 3638]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I99 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I99 FirstGlance]. <br>
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</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>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4i99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i99 OCA], [https://pdbe.org/4i99 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i99 RCSB], [https://www.ebi.ac.uk/pdbsum/4i99 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i99 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SMC_PYRFU SMC_PYRFU] Required for chromosome condensation and partitioning (By similarity). Binds single-stranded but not double-stranded DNA.[HAMAP-Rule:MF_01894]
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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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Authors: Shin, H., Soh, Y., Oh, B.
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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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Description: Crystal structure of the SmcHead bound to the C-winged helix domain of ScpA
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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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<div class="pdbe-citations 4i99" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Condensin|Condensin]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Pyrococcus furiosus DSM 3638]]
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[[Category: Oh BH]]
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[[Category: Shin HC]]
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[[Category: Soh YM]]

Current revision

Crystal structure of the SmcHead bound to the C-winged helix domain of ScpA

PDB ID 4i99

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