SMC_hingeSMC proteins Flexible Hinge Domain |
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| SMART accession number: | SM00968
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| Description: |
This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction (PUBMED:12411491). |
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| Interpro abstract (IPR010935): |
This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction [(PUBMED:12411491)].
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| GO process: | chromosome organization (GO:0051276) |
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| GO component: | chromosome (GO:0005694) |
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| GO function: | protein binding (GO:0005515), ATP binding (GO:0005524) |
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| Family alignment: |
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There are 1929
SMC_hinge domains in 1929 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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- Cellular role (predicted cellular role)
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Cellular role: chromatin
- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Hirano M, Hirano T
- Hinge-mediated dimerization of SMC protein is essential for its dynamicinteraction with DNA.
- EMBO J. 2002; 21: 5733-44
- Display abstract
Structural maintenance of chromosomes (SMC) proteins play central roles inregulating higher order chromosome dynamics from bacteria to humans. Asjudged by electron microscopy, the SMC homodimer from Bacillus subtilis(BsSMC) is composed of two antiparallel, coiled-coil arms with a flexiblehinge. Site-directed cross-linking experiments show here that dimerizationof BsSMC is mediated by a hinge-hinge interaction between self-foldedmonomers. This architecture is conserved in the eukaryotic SMC2-SMC4heterodimer. Analysis of different deletion mutants of BsSMC unexpectedlyreveals that the major DNA-binding activity does not reside in thecatalytic ATPase domains located at the ends of a dimer. Instead, pointmutations in the hinge domain that disturb dimerization of BsSMCdrastically reduce its ability to interact with DNA. Proper hinge functionis essential for BsSMC to recognize distinct DNA topology, and mutantproteins with altered hinge angles cross-link double-stranded DNA in anucleotide-dependent manner. We propose that the hinge domain of SMCproteins is not a simple dimerization site, but rather it acts as anessential determinant of dynamic SMC-DNA interactions.
- Structure (3D structures containing this domain)
3D Structures of SMC_hinge domains in PDB
| PDB code | Main view | Title | | 1gxj |  | Smc hinge domain from t. maritima w/o coiled coil |
| 1gxk |  | Smc hinge domain from t. maritima w/o coiled coil, p212121 crystal form |
| 1gxl |  | Smc hinge domain from t. maritima with coiled coil |
- Links (links to other resources describing this domain)
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