1sce
From Proteopedia
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CRYSTAL STRUCTURE OF THE CELL CYCLE REGULATORY PROTEIN SUC1 REVEALS A NOVEL BETA-HINGE CONFORMATIONAL SWITCH
Overview
The Schizosaccharomyces pombe cell cycle-regulatory protein suc1, named as, the suppressor of cdc2 temperature-sensitive mutations, is essential for, cell cycle progression. To understand suc1 structure-function, relationships and to help resolve conflicting interpretations of suc1, function based on genetic studies of suc1 and its functional homologs in, both lower and higher eukaryotes, we have determined the crystal structure, of the beta-interchanged suc1 dimer. Each domain consists of three, alpha-helices and a four-stranded beta-sheet, completed by the interchange, of terminal beta-strands between the two subunits. This beta-interchanged, suc1 dimer, when compared with the beta-hairpin single-domain folds of, suc1, reveals a beta-hinge motif formed by the conserved amino acid, sequence HVPEPH. This beta-hinge mediates the subunit conformation and, assembly of suc1: closing produces the intrasubunit beta-hairpin and, single-domain fold, whereas opening leads to the intersubunit beta-strand, interchange and interlocked dimer assembly reported here. This, conformational switch markedly changes the surface accessibility of, sequence-conserved residues available for recognition of cyclin-dependent, kinase, suggesting a structural mechanism for beta-hinge-mediated, regulation of suc1 biological function. Thus, suc1 belongs to the family, of domain-swapping proteins, consisting of intertwined and dimeric protein, structures in which the dual assembly modes regulate their function.
About this Structure
1SCE is a Single protein structure of sequence from Schizosaccharomyces pombe with CL as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the cell cycle-regulatory protein suc1 reveals a beta-hinge conformational switch., Bourne Y, Arvai AS, Bernstein SL, Watson MH, Reed SI, Endicott JE, Noble ME, Johnson LN, Tainer JA, Proc Natl Acad Sci U S A. 1995 Oct 24;92(22):10232-6. PMID:7479758
Page seeded by OCA on Wed Nov 21 02:16:19 2007
