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5h67

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

Structural highlights

5h67 is a 3 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.072035Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5h67"

Categories: Bacillus subtilis subsp. subtilis str. 168 | Large Structures | Hirano T | Kamada K

@@ Line 1: / Line 1: @@
 ==Crystal structure of the Bacillus subtilis SMC head domain complexed with the cognate ScpA C-terminal domain and soaked ATP==
-<StructureSection load='5h67' size='340' side='right' caption='[[5h67]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
+<StructureSection load='5h67' size='340' side='right'caption='[[5h67]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5h67]] is a 3 chain structure. 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]] 2.072035&#8491;</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='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>
+<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>
 </table>
 == 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;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Hirano, T]]
+[[Category: Bacillus subtilis subsp. subtilis str. 168]]
-[[Category: Kamada, K]]
+[[Category: Large Structures]]
-[[Category: Dna binding protein-cell cycle complex]]
+[[Category: Hirano T]]
-[[Category: Smc protein]]
+[[Category: Kamada K]]

5h67

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Current revision

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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