This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
5h67
From Proteopedia
(Difference between revisions)
| Line 10: | Line 10: | ||
== 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] | [[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] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5h67" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 06:27, 19 April 2017
Crystal structure of the Bacillus subtilis SMC head domain complexed with the cognate ScpA C-terminal domain and soaked ATP
| |||||||||||
