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| | <StructureSection load='5h67' size='340' side='right'caption='[[5h67]], [[Resolution|resolution]] 2.07Å' scene=''> | | <StructureSection load='5h67' size='340' side='right'caption='[[5h67]], [[Resolution|resolution]] 2.07Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5h67]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H67 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H67 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5h67]] 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=5H67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H67 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.072035Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h66|5h66]], [[5h68|5h68]], [[5h69|5h69]], [[3w6j|3w6j]], [[3w6k|3w6k]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">smc, ylqA, BSU15940 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU]), scpA, ypuG, BSU23220 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</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=5h67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h67 OCA], [https://pdbe.org/5h67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h67 RCSB], [https://www.ebi.ac.uk/pdbsum/5h67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h67 ProSAT]</span></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=5h67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h67 OCA], [http://pdbe.org/5h67 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h67 RCSB], [http://www.ebi.ac.uk/pdbsum/5h67 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h67 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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] | + | [https://www.uniprot.org/uniprot/SMC_BACSU SMC_BACSU] Required for chromosome condensation and partitioning.<ref>PMID:9573042</ref> <ref>PMID:9701812</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacsu]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hirano, T]] | + | [[Category: Hirano T]] |
| - | [[Category: Kamada, K]] | + | [[Category: Kamada K]] |
| - | [[Category: Dna binding protein-cell cycle complex]]
| + | |
| - | [[Category: Smc protein]]
| + | |
| Structural highlights
Function
SMC_BACSU Required for chromosome condensation and partitioning.[1] [2]
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Britton RA, Lin DC, Grossman AD. Characterization of a prokaryotic SMC protein involved in chromosome partitioning. Genes Dev. 1998 May 1;12(9):1254-9. PMID:9573042
- ↑ Moriya S, Tsujikawa E, Hassan AK, Asai K, Kodama T, Ogasawara N. A Bacillus subtilis gene-encoding protein homologous to eukaryotic SMC motor protein is necessary for chromosome partition. Mol Microbiol. 1998 Jul;29(1):179-87. PMID:9701812
- ↑ Kamada K, Su'etsugu M, Takada H, Miyata M, Hirano T. Overall Shapes of the SMC-ScpAB Complex Are Determined by Balance between Constraint and Relaxation of Its Structural Parts. Structure. 2017 Apr 4;25(4):603-616.e4. doi: 10.1016/j.str.2017.02.008. Epub 2017, Mar 9. PMID:28286005 doi:http://dx.doi.org/10.1016/j.str.2017.02.008
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