1ow5

From Proteopedia

(Difference between revisions)

Current revision

NMR structure of the Saccharomyces cerevisiae SAM (Sterile Alpha Motif) domain

Structural highlights

1ow5 is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

STE11_YEAST Serine/threonine protein kinase required for cell-type-specific transcription and signal transduction in yeast. It is thought that it phosphorylates the STE7 protein kinase which itself, phosphorylates the FUS3 and or KSS1 kinases.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Ste11 is a MAPKKK from Saccharomyces cerevisiae that helps mediate the response to mating pheromone and the ability to thrive in high-salt environments. These diverse functions are facilitated by a direct interaction between the SAM domain of Ste11 with the SAM domain of its regulatory partner, Ste50. We have solved the NMR structure of the Ste11 SAM domain (PDB 1OW5), which reveals a compact, five alpha-helix bundle and a high degree of structural similarity to the Polyhomeotic SAM domain. The combined study of Ste11 SAM rotational correlation times and crosslinking to Ste50-SAM has suggested a mode through which Ste11-SAM oligomerizes and selectively associates with Ste50-SAM. To probe homotypic and heterotypic interations, Ste11-SAM variants each containing a substitution of a surface-exposed hydrophobic residue were constructed. An I59R variant of Ste11-SAM, disrupted binding to Ste50-SAM in vitro. Yeast expressing full-length Ste11-I59R could neither respond to mating pheromone nor thrive in high salt media-demonstrating that the interaction between Ste11 and Ste50 SAM domains is a prerequisite for key signal transduction events.

The solution structure of the S.cerevisiae Ste11 MAPKKK SAM domain and its partnership with Ste50.,Kwan JJ, Warner N, Pawson T, Donaldson LW J Mol Biol. 2004 Sep 10;342(2):681-93. PMID:15327964^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Cairns BR, Ramer SW, Kornberg RD. Order of action of components in the yeast pheromone response pathway revealed with a dominant allele of the STE11 kinase and the multiple phosphorylation of the STE7 kinase. Genes Dev. 1992 Jul;6(7):1305-18. PMID:1628833
↑ Zarrinpar A, Bhattacharyya RP, Nittler MP, Lim WA. Sho1 and Pbs2 act as coscaffolds linking components in the yeast high osmolarity MAP kinase pathway. Mol Cell. 2004 Jun 18;14(6):825-32. PMID:15200959 doi:http://dx.doi.org/10.1016/j.molcel.2004.06.011
↑ Kwan JJ, Warner N, Pawson T, Donaldson LW. The solution structure of the S.cerevisiae Ste11 MAPKKK SAM domain and its partnership with Ste50. J Mol Biol. 2004 Sep 10;342(2):681-93. PMID:15327964 doi:10.1016/j.jmb.2004.06.064

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ow5"

Categories: Large Structures | Saccharomyces cerevisiae | Donaldson LW

@@ Line 1: / Line 1: @@
-[[Image:1ow5.gif|left|200px]]
-<!--
+==NMR structure of the Saccharomyces cerevisiae SAM (Sterile Alpha Motif) domain==
-The line below this paragraph, containing "STRUCTURE_1ow5", creates the "Structure Box" on the page.
+<StructureSection load='1ow5' size='340' side='right'caption='[[1ow5]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1ow5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OW5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OW5 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
--->
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ow5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ow5 OCA], [https://pdbe.org/1ow5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ow5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ow5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ow5 ProSAT]</span></td></tr>
-{{STRUCTURE_1ow5|  PDB=1ow5  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/STE11_YEAST STE11_YEAST] Serine/threonine protein kinase required for cell-type-specific transcription and signal transduction in yeast. It is thought that it phosphorylates the STE7 protein kinase which itself, phosphorylates the FUS3 and or KSS1 kinases.<ref>PMID:1628833</ref> <ref>PMID:15200959</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ow/1ow5_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ow5 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Ste11 is a MAPKKK from Saccharomyces cerevisiae that helps mediate the response to mating pheromone and the ability to thrive in high-salt environments. These diverse functions are facilitated by a direct interaction between the SAM domain of Ste11 with the SAM domain of its regulatory partner, Ste50. We have solved the NMR structure of the Ste11 SAM domain (PDB 1OW5), which reveals a compact, five alpha-helix bundle and a high degree of structural similarity to the Polyhomeotic SAM domain. The combined study of Ste11 SAM rotational correlation times and crosslinking to Ste50-SAM has suggested a mode through which Ste11-SAM oligomerizes and selectively associates with Ste50-SAM. To probe homotypic and heterotypic interations, Ste11-SAM variants each containing a substitution of a surface-exposed hydrophobic residue were constructed. An I59R variant of Ste11-SAM, disrupted binding to Ste50-SAM in vitro. Yeast expressing full-length Ste11-I59R could neither respond to mating pheromone nor thrive in high salt media-demonstrating that the interaction between Ste11 and Ste50 SAM domains is a prerequisite for key signal transduction events.
-'''NMR structure of the Saccharomyces cerevisiae SAM (Sterile Alpha Motif) domain'''
+The solution structure of the S.cerevisiae Ste11 MAPKKK SAM domain and its partnership with Ste50.,Kwan JJ, Warner N, Pawson T, Donaldson LW J Mol Biol. 2004 Sep 10;342(2):681-93. PMID:15327964<ref>PMID:15327964</ref>
-==Overview==
-Ste11 is a MAPKKK from Saccharomyces cerevisiae that helps mediate the response to mating pheromone and the ability to thrive in high-salt environments. These diverse functions are facilitated by a direct interaction between the SAM domain of Ste11 with the SAM domain of its regulatory partner, Ste50. We have solved the NMR structure of the Ste11 SAM domain (PDB 1OW5), which reveals a compact, five alpha-helix bundle and a high degree of structural similarity to the Polyhomeotic SAM domain. The combined study of Ste11 SAM rotational correlation times and crosslinking to Ste50-SAM has suggested a mode through which Ste11-SAM oligomerizes and selectively associates with Ste50-SAM. To probe homotypic and heterotypic interations, Ste11-SAM variants each containing a substitution of a surface-exposed hydrophobic residue were constructed. An I59R variant of Ste11-SAM, disrupted binding to Ste50-SAM in vitro. Yeast expressing full-length Ste11-I59R could neither respond to mating pheromone nor thrive in high salt media-demonstrating that the interaction between Ste11 and Ste50 SAM domains is a prerequisite for key signal transduction events.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-OW5 is a [[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=1OW5 OCA].
+</div>
+<div class="pdbe-citations 1ow5" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-The solution structure of the S.cerevisiae Ste11 MAPKKK SAM domain and its partnership with Ste50., Kwan JJ, Warner N, Pawson T, Donaldson LW, J Mol Biol. 2004 Sep 10;342(2):681-93. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15327964 15327964]
+*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Single protein]]
+[[Category: Donaldson LW]]
-[[Category: Donaldson, L W.]]
-[[Category: Map kinase]]
-[[Category: Mapkkk]]
-[[Category: Pointed domain]]
-[[Category: Sam domain]]
-[[Category: Scm domain]]
-[[Category: Ste50 regulator]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:20:53 2008''

1ow5

From Proteopedia

Current revision

NMR structure of the Saccharomyces cerevisiae SAM (Sterile Alpha Motif) domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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