5h66

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==Crystal structure of the Bacillus subtilis SMC head domain complexed with the cognate ScpA C-terminal domain==
==Crystal structure of the Bacillus subtilis SMC head domain complexed with the cognate ScpA C-terminal domain==
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<StructureSection load='5h66' size='340' side='right' caption='[[5h66]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
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<StructureSection load='5h66' size='340' side='right'caption='[[5h66]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5h66]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H66 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H66 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5h66]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H66 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H66 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h67|5h67]], [[5h68|5h68]], [[5h69|5h69]], [[3w6j|3w6j]], [[3w6k|3w6k]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8219477&#8491;</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=5h66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h66 OCA], [http://pdbe.org/5h66 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h66 RCSB], [http://www.ebi.ac.uk/pdbsum/5h66 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h66 ProSAT]</span></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=5h66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h66 OCA], [https://pdbe.org/5h66 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h66 RCSB], [https://www.ebi.ac.uk/pdbsum/5h66 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h66 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SMC_BACSU SMC_BACSU]] Required for chromosome condensation and partitioning.<ref>PMID:9573042</ref> <ref>PMID:9701812</ref> [[http://www.uniprot.org/uniprot/SCPA_BACSU SCPA_BACSU]] 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.[HAMAP-Rule:MF_01805]
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[https://www.uniprot.org/uniprot/SMC_BACSU SMC_BACSU] Required for chromosome condensation and partitioning.<ref>PMID:9573042</ref> <ref>PMID:9701812</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The SMC-ScpAB complex plays a crucial role in chromosome organization and segregation in many bacteria. It is composed of a V-shaped SMC dimer and an ScpAB subcomplex that bridges the two Structural Maintenance of Chromosomes (SMC) head domains. Despite its functional significance, the mechanistic details of SMC-ScpAB remain obscure. Here we provide evidence that ATP-dependent head-head engagement induces a lever movement of the SMC neck region, which might help to separate juxtaposed coiled-coil arms. Binding of the ScpA N-terminal domain (NTD) to the SMC neck region is negatively regulated by the ScpB C-terminal domain. Mutations in the ScpA NTD compromise this regulation and profoundly affect the overall shape of the complex. The SMC hinge domain is structurally relaxed when free from coiled-coil juxtaposition. Taken together, we propose that the structural parts of SMC-ScpAB are subjected to the balance between constraint and relaxation, cooperating to modulate dynamic conformational changes of the whole complex.
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Overall Shapes of the SMC-ScpAB Complex Are Determined by Balance between Constraint and Relaxation of Its Structural Parts.,Kamada K, Su'etsugu M, Takada H, Miyata M, Hirano T Structure. 2017 Apr 4;25(4):603-616.e4. doi: 10.1016/j.str.2017.02.008. Epub 2017, Mar 9. PMID:28286005<ref>PMID:28286005</ref>
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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 5h66" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Hirano, T]]
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[[Category: Bacillus subtilis subsp. subtilis str. 168]]
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[[Category: Kamada, K]]
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[[Category: Large Structures]]
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[[Category: Dna binding protein-cell cycle complex]]
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[[Category: Hirano T]]
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[[Category: Smc protein]]
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[[Category: Kamada K]]

Current revision

Crystal structure of the Bacillus subtilis SMC head domain complexed with the cognate ScpA C-terminal domain

PDB ID 5h66

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