3fze

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<StructureSection load='3fze' size='340' side='right'caption='[[3fze]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='3fze' size='340' side='right'caption='[[3fze]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3fze]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FZE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3fze]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FZE FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NUL3, STE5, YD8557.12, YDR103W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.601&#8491;</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=3fze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fze OCA], [https://pdbe.org/3fze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fze RCSB], [https://www.ebi.ac.uk/pdbsum/3fze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fze ProSAT]</span></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=3fze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fze OCA], [https://pdbe.org/3fze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fze RCSB], [https://www.ebi.ac.uk/pdbsum/3fze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fze ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/STE5_YEAST STE5_YEAST]] Component of the pheromone signal transduction pathway. It mediates pheromone signals acting between STE20 and STE11. It is absolutely required for pheromone-induced transcription of FUS1. May play a role in cell-cycle arrest in response to pheromone.
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[https://www.uniprot.org/uniprot/STE5_YEAST STE5_YEAST] Component of the pheromone signal transduction pathway. It mediates pheromone signals acting between STE20 and STE11. It is absolutely required for pheromone-induced transcription of FUS1. May play a role in cell-cycle arrest in response to pheromone.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The scaffold protein Ste5 is required to properly direct signaling through the yeast mating pathway to the mitogen-activated protein kinase (MAPK), Fus3. Scaffolds are thought to function by tethering kinase and substrate in proximity. We find, however, that the previously identified Fus3-binding site on Ste5 is not required for signaling, suggesting an alternative mechanism controls Fus3's activation by the MAPKK Ste7. Reconstituting MAPK signaling in vitro, we find that Fus3 is an intrinsically poor substrate for Ste7, although the related filamentation MAPK, Kss1, is an excellent substrate. We identify and structurally characterize a domain in Ste5 that catalytically unlocks Fus3 for phosphorylation by Ste7. This domain selectively increases the k(cat) of Ste7--&gt;Fus3 phosphorylation but has no effect on Ste7--&gt;Kss1 phosphorylation. The dual requirement for both Ste7 and this Ste5 domain in Fus3 activation explains why Fus3 is selectively activated by the mating pathway and not by other pathways that also utilize Ste7.
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The Ste5 scaffold directs mating signaling by catalytically unlocking the Fus3 MAP kinase for activation.,Good M, Tang G, Singleton J, Remenyi A, Lim WA Cell. 2009 Mar 20;136(6):1085-97. PMID:19303851<ref>PMID:19303851</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3fze" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 18824]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Good, M C]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Lim, W A]]
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[[Category: Good MC]]
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[[Category: Remenyi, A]]
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[[Category: Lim WA]]
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[[Category: Singleton, J]]
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[[Category: Remenyi A]]
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[[Category: Tang, G]]
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[[Category: Singleton J]]
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[[Category: Alpha/beta/alpha]]
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[[Category: Tang G]]
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[[Category: Cytoplasm]]
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[[Category: Pheromone response]]
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[[Category: Phosphoprotein]]
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[[Category: Protein binding]]
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Current revision

Structure of the 'minimal scaffold' (ms) domain of Ste5 that cocatalyzes Fus3 phosphorylation by Ste7

PDB ID 3fze

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