5h68

<table><tr><td colspan='2'>[[5h68]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_stearothermophilus_10 Bacillus stearothermophilus 10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H68 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H68 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h66|5h66]], [[5h67|5h67]], [[5h69|5h69]], [[3w6j|3w6j]], [[3w6k|3w6k]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">smc, GT50_02560 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272567 Bacillus stearothermophilus 10])</td></tr>

<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=5h68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h68 OCA], [http://pdbe.org/5h68 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h68 RCSB], [http://www.ebi.ac.uk/pdbsum/5h68 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h68 ProSAT]</span></td></tr>

== Function ==

[[http://www.uniprot.org/uniprot/A0A0K2H586_GEOSE A0A0K2H586_GEOSE]] Required for chromosome condensation and partitioning.[HAMAP-Rule:MF_01894]

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== Publication Abstract from PubMed ==

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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 5h68" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillus stearothermophilus 10]]

[[Category: Hirano, T]]

[[Category: Kamada, K]]

[[Category: Smc protein]]