2HJN

Structural and functional analysis of Saccharomyces cerevisiae Mob1

Summary for 2HJN

• Entry DOI: 10.2210/pdb2hjn/pdb
• Descriptor: Maintenance of ploidy protein MOB1, ZINC ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: homodimer, cell cycle
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm: P40484
• Total number of polymer chains: 1
• Total formula weight: 27883.14

Authors

Mrkobrada, S.,Ceccarelli, D.F.,Sicheri, F. (deposition date: 2006-06-30, release date: 2006-09-26, Last modification date: 2024-10-30)

Primary citation

Mrkobrada, S.,Boucher, L.,Ceccarelli, D.F.,Tyers, M.,Sicheri, F.
Structural and Functional Analysis of Saccharomyces cerevisiae Mob1.
J.Mol.Biol., 362:430-440, 2006

PubMed Abstract: 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.

PubMed: 16934835
DOI: 10.1016/j.jmb.2006.07.007

Experimental method

X-RAY DIFFRACTION (2 Å)