1zth | pdb_00001zth
Crystal Structure of A.fulgidus Rio1 serine protein kinase bound to ADP and Manganese ion
|
Overview
Rio1 is the founding member of the RIO family of atypical serine kinases, that are universally present in all organisms from archaea to mammals., Activity of Rio1 was shown to be absolutely essential in Saccharomyces, cerevisiae for the processing of 18S ribosomal RNA, as well as for proper, cell cycle progression and chromosome maintenance. We determined, high-resolution crystal structures of Archaeoglobus fulgidus Rio1 in the, presence and absence of bound nucleotides. Crystallization of Rio1 in the, presence of ATP or ADP and manganese ions demonstrated major, conformational changes in the active site, compared with the uncomplexed, protein. Comparisons of the structure of Rio1 with the previously, determined structure of the Rio2 kinase defined the minimal RIO domain and, the distinct features of the RIO subfamilies. We report here that Ser108, represents the sole autophosphorylation site of A. fulgidus Rio1 and have, therefore established its putative peptide substrate. In addition, we show, that a mutant enzyme that cannot be autophosphorylated can still, phosphorylate an inactive form of Rio1, as well as a number of typical, kinase substrates.
About this Structure
1ZTH is a Single protein structure of sequence from Archaeoglobus fulgidus with MN and ADP as ligands. Full crystallographic information is available from OCA.
Reference
Structure and activity of the atypical serine kinase Rio1., Laronde-Leblanc N, Guszczynski T, Copeland T, Wlodawer A, FEBS J. 2005 Jul;272(14):3698-713. PMID:16008568
Page seeded by OCA on Tue Jan 29 17:42:35 2008
