1GXK

SMC hinge domain from T. maritima w/o coiled coil, P212121 crystal form

Summary for 1GXK

• Entry DOI: 10.2210/pdb1gxk/pdb
• Related: 1E69 1GXJ 1GXL
• Descriptor: CHROMOSOME SEGREGATION SMC PROTEIN (1 entity in total)
• Functional Keywords: chromosome segregation, smc dimerisation domain, anti parallel coiled coil, smc proteins, complete proteome.
• Biological source: THERMOTOGA MARITIMA
• Cellular location: Cytoplasm : Q9X0R4
• Total number of polymer chains: 4
• Total formula weight: 83379.16

Authors

Lowe, J.,Haering, C.,Nasmyth, K. (deposition date: 2002-04-07, release date: 2002-04-29, Last modification date: 2023-12-13)

Primary citation

Haering, C.,Lowe, J.,Hochwagen, A.,Nasmyth, K.
Molecular Architecture of Smc Proteins and the Yeast Cohesin Complex
Mol.Cell, 9:773-, 2002

PubMed Abstract: 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.

PubMed: 11983169
DOI: 10.1016/S1097-2765(02)00515-4

Experimental method

X-RAY DIFFRACTION (3 Å)