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2WD5

SMC hinge heterodimer (Mouse)

Summary for 2WD5
Entry DOI10.2210/pdb2wd5/pdb
DescriptorSTRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 1A, STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3 (3 entities in total)
Functional Keywordsdna damage, cell cycle, cell division
Biological sourceMUS MUSCULUS (MOUSE)
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Cellular locationNucleus: Q9CU62 Q9CW03
Total number of polymer chains2
Total formula weight51167.70
Authors
Michie, K.A.,Haering, C.H.,Nasmyth, K.,Lowe, J. (deposition date: 2009-03-20, release date: 2010-08-11, Last modification date: 2024-05-08)
Primary citationKurze, A.,Michie, K.A.,Dixon, S.E.,Mishra, A.,Itoh, T.,Khalid, S.,Strmecki, L.,Shirahige, K.,Haering, C.H.,Lowe, J.,Nasmyth, K.
A Positively Charged Channel within the Smc1/Smc3 Hinge Required for Sister Chromatid Cohesion.
Embo J., 30:364-, 2011
Cited by
PubMed Abstract: Cohesin's structural maintenance of chromosome 1 (Smc1) and Smc3 are rod-shaped proteins with 50-nm long intra-molecular coiled-coil arms with a heterodimerization domain at one end and an ABC-like nucleotide-binding domain (NBD) at the other. Heterodimerization creates V-shaped molecules with a hinge at their centre. Inter-connection of NBDs by Scc1 creates a tripartite ring within which, it is proposed, sister DNAs are entrapped. To investigate whether cohesin's hinge functions as a possible DNA entry gate, we solved the crystal structure of the hinge from Mus musculus, which like its bacterial counterpart is characterized by a pseudo symmetric heterodimeric torus containing a small channel that is positively charged. Mutations in yeast Smc1 and Smc3 that together neutralize the channel's charge have little effect on dimerization or association with chromosomes, but are nevertheless lethal. Our finding that neutralization reduces acetylation of Smc3, which normally occurs during replication and is essential for cohesion, suggests that the positively charged channel is involved in a major conformational change during S phase.
PubMed: 21139566
DOI: 10.1038/EMBOJ.2010.315
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

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