2ixp | pdb_00002ixp
CRYSTAL STRUCTURE OF THE PP2A PHOSPHATASE ACTIVATOR YPA1 PTPA1 IN COMPLEX WITH MODEL SUBSTRATE
|
Overview
PTPA, an essential and specific activator of protein phosphatase 2A, (PP2A), functions as a peptidyl prolyl isomerase (PPIase). We present here, the crystal structures of human PTPA and of the two yeast orthologs (Ypa1, and Ypa2), revealing an all alpha-helical protein fold that is radically, different from other PPIases. The protein is organized into two domains, separated by a groove lined by highly conserved residues. To understand, the molecular mechanism of PTPA activity, Ypa1 was cocrystallized with a, proline-containing PPIase peptide substrate. In the complex, the peptide, binds at the interface of a peptide-induced dimer interface. Conserved, residues of the interdomain groove contribute to the peptide binding site, and dimer interface. Structure-guided mutational studies showed ... [(full description)]
About this Structure
2IXP is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with SO4, CL and SIN as [ligands]. Full crystallographic information is available from [OCA].
Reference
Crystal structure of the PP2A phosphatase activator: implications for its PP2A-specific PPIase activity., Leulliot N, Vicentini G, Jordens J, Quevillon-Cheruel S, Schiltz M, Barford D, van Tilbeurgh H, Goris J, Mol Cell. 2006 Aug 4;23(3):413-24. PMID:16885030
Page seeded by OCA on Mon Oct 29 19:58:16 2007
