1z1v: Difference between revisions

Revision as of 17:11, 21 February 2008

NMR structure of the Saccharomyces cerevisiae Ste50 SAM domain

OverviewOverview

In Saccharomyces cerevisiae, signal transduction through pathways governing mating, osmoregulation, and nitrogen starvation depends upon a direct interaction between the sterile alpha motif (SAM) domains of the Ste11 mitogen-activated protein kinase kinase kinase (MAPKKK) and its regulator Ste50. Previously, we solved the NMR structure of the SAM domain from Ste11 and identified two mutants that diminished binding to the Ste50 SAM domain. Building upon the Ste11 study, we present the NMR structure of the monomeric Ste50 SAM domain and a series of mutants bearing substitutions at surface-exposed hydrophobic amino acid residues. The mid-loop (ML) region of Ste11-SAM, defined by helices H3 and H4 and the end-helix (EH) region of Ste50-SAM, defined by helix H5, were sensitive to substitution, indicating that these two surfaces contribute to the high-affinity interaction. The combination of two mutants, Ste11-SAM-L72R and Ste50-SAM-L69R, formed a high-affinity heterodimer unencumbered by competing homotypic interactions that had prevented earlier NMR studies of the wild-type complex. Yeast bearing mutations that prevented the heterotypic Ste11-Ste50 association in vitro presented signaling defects in the mating and high-osmolarity growth pathways.

About this StructureAbout this Structure

1Z1V is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Saccharomyces cerevisiae Ste50 binds the MAPKKK Ste11 through a head-to-tail SAM domain interaction., Kwan JJ, Warner N, Maini J, Chan Tung KW, Zakaria H, Pawson T, Donaldson LW, J Mol Biol. 2006 Feb 10;356(1):142-54. Epub 2005 Nov 28. PMID:16337230

Page seeded by OCA on Thu Feb 21 16:11:25 2008

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OCA

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-[[Image:1z1v.gif|left|200px]]<br /><applet load="1z1v" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1z1v" />
 '''NMR structure of the Saccharomyces cerevisiae Ste50 SAM domain'''<br />
 ==Overview==
-In Saccharomyces cerevisiae, signal transduction through pathways, governing mating, osmoregulation, and nitrogen starvation depends upon a, direct interaction between the sterile alpha motif (SAM) domains of the, Ste11 mitogen-activated protein kinase kinase kinase (MAPKKK) and its, regulator Ste50. Previously, we solved the NMR structure of the SAM domain, from Ste11 and identified two mutants that diminished binding to the Ste50, SAM domain. Building upon the Ste11 study, we present the NMR structure of, the monomeric Ste50 SAM domain and a series of mutants bearing, substitutions at surface-exposed hydrophobic amino acid residues. The, mid-loop (ML) region of Ste11-SAM, defined by helices H3 and H4 and the, end-helix (EH) region of Ste50-SAM, defined by helix H5, were sensitive to, substitution, indicating that these two surfaces contribute to the, high-affinity interaction. The combination of two mutants, Ste11-SAM-L72R, and Ste50-SAM-L69R, formed a high-affinity heterodimer unencumbered by, competing homotypic interactions that had prevented earlier NMR studies of, the wild-type complex. Yeast bearing mutations that prevented the, heterotypic Ste11-Ste50 association in vitro presented signaling defects, in the mating and high-osmolarity growth pathways.
+In Saccharomyces cerevisiae, signal transduction through pathways governing mating, osmoregulation, and nitrogen starvation depends upon a direct interaction between the sterile alpha motif (SAM) domains of the Ste11 mitogen-activated protein kinase kinase kinase (MAPKKK) and its regulator Ste50. Previously, we solved the NMR structure of the SAM domain from Ste11 and identified two mutants that diminished binding to the Ste50 SAM domain. Building upon the Ste11 study, we present the NMR structure of the monomeric Ste50 SAM domain and a series of mutants bearing substitutions at surface-exposed hydrophobic amino acid residues. The mid-loop (ML) region of Ste11-SAM, defined by helices H3 and H4 and the end-helix (EH) region of Ste50-SAM, defined by helix H5, were sensitive to substitution, indicating that these two surfaces contribute to the high-affinity interaction. The combination of two mutants, Ste11-SAM-L72R and Ste50-SAM-L69R, formed a high-affinity heterodimer unencumbered by competing homotypic interactions that had prevented earlier NMR studies of the wild-type complex. Yeast bearing mutations that prevented the heterotypic Ste11-Ste50 association in vitro presented signaling defects in the mating and high-osmolarity growth pathways.
 ==About this Structure==
-Z1V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z1V OCA].
+Z1V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z1V OCA].
 ==Reference==
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 [[Category: Saccharomyces cerevisiae]]
 [[Category: Single protein]]
-[[Category: Donaldson, L.W.]]
+[[Category: Donaldson, L W.]]
-[[Category: Kwan, J.J.]]
+[[Category: Kwan, J J.]]
 [[Category: Maini, J.]]
 [[Category: Pawson, T.]]
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 [[Category: sam domain]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:11:46 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:11:25 2008''