1gxk: Difference between revisions

New page: left|200px<br /><applet load="1gxk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gxk, resolution 3.0Å" /> '''SMC HINGE DOMAIN FROM...
 
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[[Image:1gxk.gif|left|200px]]<br /><applet load="1gxk" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1gxk.gif|left|200px]]<br /><applet load="1gxk" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1gxk, resolution 3.0&Aring;" />
caption="1gxk, resolution 3.0&Aring;" />
'''SMC HINGE DOMAIN FROM T. MARITIMA W/O COILED COIL, P212121 CRYSTAL FORM'''<br />
'''SMC HINGE DOMAIN FROM T. MARITIMA W/O COILED COIL, P212121 CRYSTAL FORM'''<br />


==Overview==
==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.
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==
==About this Structure==
1GXK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GXK OCA].  
1GXK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GXK OCA].  


==Reference==
==Reference==
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[[Category: smc proteins]]
[[Category: smc proteins]]


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