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1w1w

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|PDB= 1w1w |SIZE=350|CAPTION= <scene name='initialview01'>1w1w</scene>, resolution 2.9&Aring;
|PDB= 1w1w |SIZE=350|CAPTION= <scene name='initialview01'>1w1w</scene>, resolution 2.9&Aring;
|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>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ATG:PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER'>ATG</scene>
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|LIGAND= <scene name='pdbligand=ATG:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>ATG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|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.]]
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[[Category: ATG]]
 
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[[Category: MG]]
 
[[Category: abc atpase]]
[[Category: abc atpase]]
[[Category: cell cycle]]
[[Category: cell cycle]]
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[[Category: mitosis]]
[[Category: mitosis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:50:56 2008''
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''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

Image:1w1w.gif


PDB ID 1w1w

Drag the structure with the mouse to rotate
, 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

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