2hjn
From Proteopedia
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Structural and functional analysis of Saccharomyces cerevisiae Mob1
Overview
The Mob proteins function as activator subunits for the Dbf2/Dbf20 family, of protein kinases. Human and Xenopus Mob1 protein structures, corresponding to the most conserved C-terminal core, but lacking the, variable N-terminal region, have been reported and provide a framework for, understanding the mechanism of Dbf2/Dbf20 regulation. Here, we report the, 2.0 A X-ray crystal structure of Saccharomyces cerevisiae Mob1 containing, both the conserved C-terminal core and the variable N-terminal region., Within the N-terminal region, three novel structural elements are, observed; namely, an alpha-helix denoted H0, a strand-like element denoted, S0 and a short beta strand denoted S-1. Helix H0 associates in an, intermolecular manner with a second Mob1 molecule to form a Mob1, homodimer. Strand S0 binds to the core domain in an intramolecular manner, across a putative Dbf2 binding site mapped by Mob1 temperature-sensitive, alleles and NMR binding experiments. In vivo functional analysis, demonstrates that Mob1 mutants that target helix H0 or its reciprocal, binding site are biologically compromised. The N-terminal region of Mob1, thus contains structural elements that are functionally important.
About this Structure
2HJN is a Single protein structure of sequence from Saccharomyces cerevisiae with ZN and SO4 as ligands. Full crystallographic information is available from OCA.
Reference
Structural and functional analysis of Saccharomyces cerevisiae Mob1., Mrkobrada S, Boucher L, Ceccarelli DF, Tyers M, Sicheri F, J Mol Biol. 2006 Sep 22;362(3):430-40. Epub 2006 Aug 24. PMID:16934835
Page seeded by OCA on Wed Nov 21 11:48:40 2007
