1gxk
From Proteopedia
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'''SMC HINGE DOMAIN FROM T. MARITIMA W/O COILED COIL, P212121 CRYSTAL FORM''' | '''SMC HINGE DOMAIN FROM T. MARITIMA W/O COILED COIL, P212121 CRYSTAL FORM''' | ||
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[[Category: Lowe, J.]] | [[Category: Lowe, J.]] | ||
[[Category: Nasmyth, K.]] | [[Category: Nasmyth, K.]] | ||
| - | [[Category: | + | [[Category: Anti parallel coiled coil]] |
| - | [[Category: | + | [[Category: Complete proteome.]] |
| - | [[Category: | + | [[Category: Smc dimerisation domain]] |
| - | [[Category: | + | [[Category: Smc protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:08:54 2008'' | |
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Revision as of 15:08, 2 May 2008
SMC HINGE DOMAIN FROM T. MARITIMA W/O COILED COIL, P212121 CRYSTAL FORM
Overview
Sister chromatids are held together by the multisubunit cohesin complex, which contains two SMC (Smc1 and Smc3) and two non-SMC (Scc1 and Scc3) proteins. The crystal structure of a bacterial SMC "hinge" region along with EM studies and biochemical experiments on yeast Smc1 and Smc3 proteins show that SMC protamers fold up individually into rod-shaped molecules. A 45 nm long intramolecular coiled coil separates the hinge region from the ATPase-containing "head" domain. Smc1 and Smc3 bind to each other via heterotypic interactions between their hinges to form a V-shaped heterodimer. The two heads of the V-shaped dimer are connected by different ends of the cleavable Scc1 subunit. Cohesin therefore forms a large proteinaceous loop within which sister chromatids might be entrapped after DNA replication.
About this Structure
1GXK is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
Molecular architecture of SMC proteins and the yeast cohesin complex., Haering CH, Lowe J, Hochwagen A, Nasmyth K, Mol Cell. 2002 Apr;9(4):773-88. PMID:11983169 Page seeded by OCA on Fri May 2 18:08:54 2008
