Condensin
From Proteopedia
(Difference between revisions)
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- | <StructureSection load=' | + | <StructureSection load='5xg3' size='340' side='right' caption='SMC head and coiled-coil domain complex with segregation and condensation protein A C-terminal and ATPγS (PDB code [[5xg3]]' scene=''> |
== Function == | == Function == | ||
- | '''Condensin''' or '''structural maintenance of chromosome protein''' (SMC) is required for correctly package and divide the cell's genome. SMC uses ATP to affect conformational changes in DNA, to correct DNA compaction, organization and segregation<ref>PMID:28181049</ref>. SMC exhibits the ability to super-coil DNA<ref>PMID:23218009</ref>. SMC of ''E. coli'' is named '''MukB''' or '''Chromosome partition protein A'''. SMC is found in species from bacteria to human. SMC | + | '''Condensin''' or '''structural maintenance of chromosome protein''' (SMC) is required for correctly package and divide the cell's genome. SMC uses ATP to affect conformational changes in DNA, to correct DNA compaction, organization and segregation<ref>PMID:28181049</ref>. SMC exhibits the ability to super-coil DNA<ref>PMID:23218009</ref>. SMC of ''E. coli'' is named '''MukB''' or '''Chromosome partition protein A'''. SMC is found in species from bacteria to human. SMC and cohesin which share structural similarities, are essential for separting the genome into daughter cells during cell division. SMC reorganizes chromsomes into their compact mitotic structure while cohesin glues replicated sister chromatids together until they split at anaphase<ref>PMID:12838344</ref>. |
== Disease == | == Disease == | ||
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**[[6qj2]] – CtSMC head domain + Brn1<br /> | **[[6qj2]] – CtSMC head domain + Brn1<br /> | ||
**[[3zgx]] – BsSMC head domain + segregation and condensation protein – ''Bacillus subtilis''<br /> | **[[3zgx]] – BsSMC head domain + segregation and condensation protein – ''Bacillus subtilis''<br /> | ||
- | **[[5xg3]] – BsSMC head domain (mutant)+ coiled-coil domain + segregation and condensation protein <br /> | + | **[[5xg3]] – BsSMC head domain (mutant)+ coiled-coil domain + segregation and condensation protein + ATPγS<br /> |
**[[1xew]] – PfSMC head domain – ''Pyrococcus furiosus''<br /> | **[[1xew]] – PfSMC head domain – ''Pyrococcus furiosus''<br /> | ||
**[[1xex]] – PfSMC head domain (mutant)<br /> | **[[1xex]] – PfSMC head domain (mutant)<br /> | ||
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**[[1qhl]] – EcMukB N-terminal 1-227 <br /> | **[[1qhl]] – EcMukB N-terminal 1-227 <br /> | ||
**[[3rpu]] – EcMukE N-terminal * MukF N-terminal <br /> | **[[3rpu]] – EcMukE N-terminal * MukF N-terminal <br /> | ||
- | **[[3euj]], [[3euk]] – MukB head domain (mutant) * MukF residues 292-443 + | + | **[[3euj]], [[3euk]] – MukB head domain (mutant) * MukF residues 292-443 + ATPγS - ''Haemophilus ducreyi''<br /> |
}} | }} | ||
== References == | == References == |
Revision as of 09:12, 3 April 2020
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3D Structures of condensin
Updated on 03-April-2020
References
- ↑ Kalitsis P, Zhang T, Marshall KM, Nielsen CF, Hudson DF. Condensin, master organizer of the genome. Chromosome Res. 2017 Mar;25(1):61-76. doi: 10.1007/s10577-017-9553-0. Epub 2017, Feb 9. PMID:28181049 doi:http://dx.doi.org/10.1007/s10577-017-9553-0
- ↑ Thadani R, Uhlmann F, Heeger S. Condensin, chromatin crossbarring and chromosome condensation. Curr Biol. 2012 Dec 4;22(23):R1012-21. doi: 10.1016/j.cub.2012.10.023. PMID:23218009 doi:http://dx.doi.org/10.1016/j.cub.2012.10.023
- ↑ Hagstrom KA, Meyer BJ. Condensin and cohesin: more than chromosome compactor and glue. Nat Rev Genet. 2003 Jul;4(7):520-34. doi: 10.1038/nrg1110. PMID:12838344 doi:http://dx.doi.org/10.1038/nrg1110
- ↑ Zhao H, Petrushenko ZM, Walker JK, Baudry J, Zgurskaya HI, Rybenkov VV. Small Molecule Condensin Inhibitors. ACS Infect Dis. 2018 Dec 14;4(12):1737-1745. doi: 10.1021/acsinfecdis.8b00222., Epub 2018 Oct 22. PMID:30346684 doi:http://dx.doi.org/10.1021/acsinfecdis.8b00222