Condensin

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: ==Your Heading Here (maybe something like 'Structure')== <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> This is a default text for you...)
Current revision (07:31, 4 April 2020) (edit) (undo)
 
(6 intermediate revisions not shown.)
Line 1: Line 1:
-
==Your Heading Here (maybe something like 'Structure')==
+
<StructureSection load='5oqn' size='340' side='right' caption='Yeast SMC subunit 2 (green) and subunit 3 (grey) complex with DNA (PDB code [[5oqn]]' scene=''>
-
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
+
-
This is a default text for your page '''Condensin'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
+
-
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
+
== Function ==
== Function ==
-
== Disease ==
+
'''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'''. '''MukE''' and '''MukF''' are associated with MukB. 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>.
== Relevance ==
== Relevance ==
 +
 +
SMC plays important role in human disease and bacterial pathogenicity and its inhibitors are studied for therapeutic purposes<ref>PMID:30346684</ref>. Mutations or removal of SMC subunits cause errors in chromosome segregation and likely cell death.
== Structural highlights ==
== Structural highlights ==
-
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
+
SMC is a multisubunit complex. In vertebrates condensin complex is formed from the association of SMC2 and SMC4 subunits. SMC2 and SMC4 contain 3 domains: head domain forming an ATPase, a long coiled-coil region and a hinge domain which facilitates SMC2/SMC4 dimerization.
</StructureSection>
</StructureSection>
Line 18: Line 17:
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
 +
{{#tree:id=OrganizedByTopic|openlevels=0|
-
*Condensin or Structural Maintenance of Chromosome Protein
+
*Condensin or Structural Maintenance of Chromosome Protein; Domains - head 1-219+983-1186
-
 
+
-
[[4u4p]] – hSMC2 hinge domain 506-666 + SMC4 hinge domain 595-752 – human <br />
+
-
[[6igx]] – hSMC subunit 2+3 <br />
+
-
[[3l51]] – SMC2 hinge domain 506-666 + SMC4 hinge domain 595-752 – mouse <br />
+
-
[[5oqq]] – ySMC subunit 2+3 – yeast<br />
+
-
[[5oqn]], [[5oqo]], [[5oqp]] – ySMC subunit 2+3 + DNA<br />
+
-
[[5oqr]] – SMC subunit 2+3 – fission yeast<br />
+
-
[[6q6e]] – CtSMC residues 112-209 – ''Chaetomium thermophilum'' - NMR<br />
+
-
[[6qj3]] – CtSMC subunit 1+2 + Brn1 <br />
+
-
[[6qj4]] – CtSMC subunit 1+2 + Brn1 + protein<br />
+
-
[[6qj0]], [[6qj1]] – CtSMC head domain <br />
+
-
[[6qj2]] – CtSMC head domain + Brn1<br />
+
-
[[3zgx]] – BsSMC head domain residues 1-219, 983-1186 + segregation and condensation protein – ''Bacillus subtilis''<br />
+
-
[[5xg3]] – BsSMC head domain residues 1-219, 983-1186 (mutant)+ coiled-coil domain + segregation and condensation protein <br />
+
-
[[1xew]] – PfSMC head domain – ''Pyrococcus furiosus''<br />
+
-
[[1xex]] – PfSMC head domain (mutant)<br />
+
-
[[4i99]] – PfSMC head domain residues 1-182, 1006-1176 + protein <br />
+
-
[[5xns]] – PfSMC head domain residues 1-219, 983-1186 + segregation and condensation protein <br />
+
-
[[5xg2]] – PySMC coiled-coil domain – ''Pyrococcus yayanosii''<br />
+
-
[[5xei]] – PySMC head+coiled-coil domains – <br />
+
 +
**[[4u4p]] – hSMC2 hinge domain 506-666 + SMC4 hinge domain 595-752 – human <br />
 +
**[[6igx]] – hSMC subunit 2+3 <br />
 +
**[[3l51]] – SMC2 hinge domain 506-666 + SMC4 hinge domain 595-752 – mouse <br />
 +
**[[5oqq]] – ySMC subunit 2+3 – yeast<br />
 +
**[[5oqn]], [[5oqo]], [[5oqp]] – ySMC subunit 2+3 + DNA<br />
 +
**[[5oqr]] – SMC subunit 2+3 – fission yeast<br />
 +
**[[6q6e]] – CtSMC residues 112-209 – ''Chaetomium thermophilum'' - NMR<br />
 +
**[[6qj3]] – CtSMC subunit 1+2 + Brn1 <br />
 +
**[[6qj4]] – CtSMC subunit 1+2 + Brn1 + protein<br />
 +
**[[6qj0]], [[6qj1]] – CtSMC head domain <br />
 +
**[[6qj2]] – CtSMC head domain + Brn1<br />
 +
**[[3zgx]] – BsSMC head domain + segregation and condensation protein – ''Bacillus subtilis''<br />
 +
**[[5xg3]] – BsSMC head domain (mutant)+ coiled-coil domain + segregation and condensation protein + ATPγS<br />
 +
**[[1xew]] – PfSMC head domain – ''Pyrococcus furiosus''<br />
 +
**[[1xex]] – PfSMC head domain (mutant)<br />
 +
**[[4i99]] – PfSMC head domain residues 1-182, 1006-1176 + protein <br />
 +
**[[5xns]] – PfSMC head domain residues 1-219, 983-1186 + segregation and condensation protein <br />
 +
**[[5xg2]] – PySMC coiled-coil domain – ''Pyrococcus yayanosii''<br />
 +
**[[5xei]] – PySMC head+coiled-coil domains – <br />
 +
*Structural Maintenance of Chromosome-related Protein or Chromosome partition protein
 +
**[[2wmm]] – EcMukB hinge domain 645-804 (mutant) - ''Escherichia coli'' <br />
 +
**[[4mn4]] – EcMukB hinge domain 645-804 * DNA topoisomerase 4 subunit A <br />
 +
**[[6h2x]], [[3ibp]] – EcMukB coiled-coil domain <br />
 +
**[[1qhl]] – EcMukB N-terminal 1-227 <br />
 +
**[[3rpu]] – EcMukE N-terminal * MukF N-terminal <br />
 +
**[[3euj]], [[3euk]] – MukB head domain (mutant) * MukF residues 292-443 + ATPγS - ''Haemophilus ducreyi''<br />
 +
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Yeast SMC subunit 2 (green) and subunit 3 (grey) complex with DNA (PDB code 5oqn

Drag the structure with the mouse to rotate

3D Structures of condensin

Updated on 04-April-2020

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel

Retrieved from "http://52.214.119.220/wiki/index.php/Condensin"
Personal tools