1PI1

Crystal structure of a human Mob1 protein; toward understanding Mob-regulated cell cycle pathways.

Summary for 1PI1

• Entry DOI: 10.2210/pdb1pi1/pdb
• Descriptor: Mob1A, ZINC ION (3 entities in total)
• Functional Keywords: mob1, mitotic exit network, mitosis, dbf2, cell cycle
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 21594.05

Authors

Stavridi, E.S.,Harris, K.G.,Huyen, Y.,Bothos, J.,Voewerd, P.M.,Stayrook, S.E.,Jeffrey, P.D.,Pavletich, N.P.,Luca, F.C. (deposition date: 2003-05-29, release date: 2003-09-30, Last modification date: 2024-05-22)

Primary citation

Stavridi, E.S.,Harris, K.G.,Huyen, Y.,Bothos, J.,Verwoerd, P.M.,Stayrook, S.E.,Pavletich, N.P.,Jeffrey, P.D.,Luca, F.C.
Crystal structure of a human mob1 protein. Toward understanding mob-regulated cell cycle pathways.
Structure, 11:1163-1170, 2003

PubMed Abstract: The Mob protein family comprises a group of highly conserved eukaryotic proteins whose founding member functions in the mitotic exit network. At the molecular level, Mob proteins act as kinase-activating subunits. We cloned a human Mob1 family member, Mob1A, and determined its three-dimensional structure by X-ray crystallography. The core of Mob1A consists of a four-helix bundle that is stabilized by a bound zinc atom. The N-terminal helix of the bundle is solvent exposed and together with adjacent secondary structure elements forms an evolutionarily conserved surface with a strong negative electrostatic potential. Several conditional mutant alleles of S. cerevisiae MOB1 target this surface and decrease its net negative charge. Interestingly, the kinases with which yeast Mob proteins interact have two conserved basic regions within their N-terminal lobe. Thus, Mob proteins may regulate their target kinases through electrostatic interactions mediated by conserved charged surfaces.

PubMed: 12962634
DOI: 10.1016/S0969-2126(03)00182-5

Experimental method

X-RAY DIFFRACTION (2 Å)