1gxj: Difference between revisions
New page: left|200px<br /><applet load="1gxj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gxj, resolution 2.0Å" /> '''SMC HINGE DOMAIN FROM... |
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[[Image:1gxj.gif|left|200px]]<br /><applet load="1gxj" size=" | [[Image:1gxj.gif|left|200px]]<br /><applet load="1gxj" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1gxj, resolution 2.0Å" /> | caption="1gxj, resolution 2.0Å" /> | ||
'''SMC HINGE DOMAIN FROM T. MARITIMA W/O COILED COIL'''<br /> | '''SMC HINGE DOMAIN FROM T. MARITIMA W/O COILED COIL'''<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) | 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== | ||
1GXJ 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:// | 1GXJ 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=1GXJ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: smc proteins]] | [[Category: smc proteins]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:55:09 2008'' | ||
Revision as of 13:55, 21 February 2008
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SMC HINGE DOMAIN FROM T. MARITIMA W/O COILED COIL
OverviewOverview
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 StructureAbout this Structure
1GXJ is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
ReferenceReference
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
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