YEAST COFILIN, ORTHORHOMBIC CRYSTAL FORMYEAST COFILIN, ORTHORHOMBIC CRYSTAL FORM
Structural highlights
1cof is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
COFI_YEAST Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton. In effect, yeast cofilin increases the rate of actin polymerization by making new ends available for actin subunit addition. Such a protein complex is important for the polarized growth of yeast cells.[1][2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
↑Iida K, Yahara I. Cooperation of two actin-binding proteins, cofilin and Aip1, in Saccharomyces cerevisiae. Genes Cells. 1999 Jan;4(1):21-32. PMID:10231390
↑Ojala PJ, Paavilainen V, Lappalainen P. Identification of yeast cofilin residues specific for actin monomer and PIP2 binding. Biochemistry. 2001 Dec 25;40(51):15562-9. PMID:11747431
