1r3b
From Proteopedia
(New page: 200px<br /><applet load="1r3b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r3b" /> '''Solution structure of xenopus laevis Mob1'''...) |
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| - | [[Image:1r3b.gif|left|200px]]<br /><applet load="1r3b" size=" | + | [[Image:1r3b.gif|left|200px]]<br /><applet load="1r3b" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1r3b" /> | caption="1r3b" /> | ||
'''Solution structure of xenopus laevis Mob1'''<br /> | '''Solution structure of xenopus laevis Mob1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Proteins of the Mob1/phocein family are found in all eukaryotic cells. In | + | Proteins of the Mob1/phocein family are found in all eukaryotic cells. In yeast, they are activating subunits of Dbf2-related protein kinases involved in cell cycle control. Despite the wide occurrence of these proteins, their biological functions remain poorly understood. Here we report the solution structure of the Mob1 protein from Xenopus laevis solved by heteronuclear multidimensional NMR. The structure reveals a fold constituted by a central left-handed four-helix bundle, one connecting helix, two flanking helices and a long flexible loop. The clustering of two Cys and two His residues, and zinc measurement by atomic absorption spectroscopy support the existence of a zinc ion binding site. Our NMR structure is in good agreement with the recently described X-ray structure of human Mob1-A. Chemical shift perturbations observed upon addition of a peptide encompassing the basic region of the N-terminal regulatory domain of NDR kinase were used to identify and map a specific interaction between Mob1 and this kinase. The chemical shift changes indicate that the main interaction occurs on the acidic and conserved surface of Mob1. This surface was previously hypothesized to be the interaction surface according to the X-ray structure and was identified as functionally important in yeast. Our data suggest that the NDR kinase is a functional Dbf2 homologue in animal cells and contributes to the understanding of the molecular function of Mob1 proteins. |
==About this Structure== | ==About this Structure== | ||
| - | 1R3B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http:// | + | 1R3B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R3B OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Dumas, C.]] | [[Category: Dumas, C.]] | ||
[[Category: Fesquet, D.]] | [[Category: Fesquet, D.]] | ||
| - | [[Category: Kajava, A | + | [[Category: Kajava, A V.]] |
[[Category: Padilla, A.]] | [[Category: Padilla, A.]] | ||
[[Category: Ponchon, L.]] | [[Category: Ponchon, L.]] | ||
[[Category: left-handed four-helix bundle]] | [[Category: left-handed four-helix bundle]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:46:32 2008'' |
Revision as of 12:46, 21 February 2008
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Solution structure of xenopus laevis Mob1
Overview
Proteins of the Mob1/phocein family are found in all eukaryotic cells. In yeast, they are activating subunits of Dbf2-related protein kinases involved in cell cycle control. Despite the wide occurrence of these proteins, their biological functions remain poorly understood. Here we report the solution structure of the Mob1 protein from Xenopus laevis solved by heteronuclear multidimensional NMR. The structure reveals a fold constituted by a central left-handed four-helix bundle, one connecting helix, two flanking helices and a long flexible loop. The clustering of two Cys and two His residues, and zinc measurement by atomic absorption spectroscopy support the existence of a zinc ion binding site. Our NMR structure is in good agreement with the recently described X-ray structure of human Mob1-A. Chemical shift perturbations observed upon addition of a peptide encompassing the basic region of the N-terminal regulatory domain of NDR kinase were used to identify and map a specific interaction between Mob1 and this kinase. The chemical shift changes indicate that the main interaction occurs on the acidic and conserved surface of Mob1. This surface was previously hypothesized to be the interaction surface according to the X-ray structure and was identified as functionally important in yeast. Our data suggest that the NDR kinase is a functional Dbf2 homologue in animal cells and contributes to the understanding of the molecular function of Mob1 proteins.
About this Structure
1R3B is a Single protein structure of sequence from Xenopus laevis. Full crystallographic information is available from OCA.
Reference
NMR solution structure of Mob1, a mitotic exit network protein and its interaction with an NDR kinase peptide., Ponchon L, Dumas C, Kajava AV, Fesquet D, Padilla A, J Mol Biol. 2004 Mar 12;337(1):167-82. PMID:15001360
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