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1w1w
From Proteopedia
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|PDB= 1w1w |SIZE=350|CAPTION= <scene name='initialview01'>1w1w</scene>, resolution 2.9Å | |PDB= 1w1w |SIZE=350|CAPTION= <scene name='initialview01'>1w1w</scene>, resolution 2.9Å | ||
|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+D'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+D'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ATG:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>ATG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w1w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w1w OCA], [http://www.ebi.ac.uk/pdbsum/1w1w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w1w RCSB]</span> | ||
}} | }} | ||
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[[Category: Lowe, J.]] | [[Category: Lowe, J.]] | ||
[[Category: Nasmyth, K.]] | [[Category: Nasmyth, K.]] | ||
| - | [[Category: ATG]] | ||
| - | [[Category: MG]] | ||
[[Category: abc atpase]] | [[Category: abc atpase]] | ||
[[Category: cell cycle]] | [[Category: cell cycle]] | ||
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[[Category: mitosis]] | [[Category: mitosis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:29:59 2008'' |
Revision as of 21:30, 30 March 2008
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| , resolution 2.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SC SMC1HD:SCC1-C COMPLEX, ATPGS
Overview
A multisubunit complex called cohesin forms a huge ring structure that mediates sister chromatid cohesion, possibly by entrapping sister DNAs following replication. Cohesin's kleisin subunit Scc1 completes the ring, connecting the ABC-like ATPase heads of a V-shaped Smc1/3 heterodimer. Proteolytic cleavage of Scc1 by separase triggers sister chromatid disjunction, presumably by breaking the Scc1 bridge. One half of the SMC-kleisin bridge is revealed here by a crystal structure of Smc1's ATPase complexed with Scc1's C-terminal domain. The latter forms a winged helix that binds a pair of beta strands in Smc1's ATPase head. Mutation of conserved residues within the contact interface destroys Scc1's interaction with Smc1/3 heterodimers and eliminates cohesin function. Interaction of Scc1's N terminus with Smc3 depends on prior C terminus connection with Smc1. There is little or no turnover of Smc1-Scc1 interactions within cohesin complexes in vivo because expression of noncleavable Scc1 after DNA replication does not hinder anaphase.
About this Structure
1W1W is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structure and stability of cohesin's Smc1-kleisin interaction., Haering CH, Schoffnegger D, Nishino T, Helmhart W, Nasmyth K, Lowe J, Mol Cell. 2004 Sep 24;15(6):951-64. PMID:15383284
Page seeded by OCA on Mon Mar 31 00:29:59 2008
