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2b9f

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Revision as of 06:32, 16 May 2018

Crystal structure of non-phosphorylated Fus3

Structural highlights

2b9f is a 1 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	2b9h, 2b9i, 2b9j
Gene:	FUS3, DAC2 (ATCC 18824)
Activity:	Transferase, with EC number 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FUS3_YEAST] Together with closely related KSS1, FUS3 is the final kinase in the signal transduction cascade regulating activation/repression of the mating and filamentation pathways, induced by pheromone and nitrogen/carbon limitation, respectively. Phosphorylated FUS3 activates the mating but suppresses the filamentation pathway, whereas activated KSS1 activates both pathways. Pheromone-activated FUS3 functions by inhibiting the binding of the transcriptional activator STE12 to filamentation specific genes while inducing its binding to and activity at mating specific genes. Non-activated FUS3 has a repressive effect on STE12 transcriptional activity. KSS1 can partially compensate for the lack of FUS3 but mating efficiency is reduced and the filamentation program is partially activated upon pheromone signaling. FUS3 phosphorylates STE7, STE5, FAR1, DIG1, DIG2 and STE12.^[1] ^[2] ^[3] ^[4]

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

Cells use a network of mitogen-activated protein kinases (MAPKs) to coordinate responses to diverse extracellular signals. Here, we examine the role of docking interactions in determining connectivity of the yeast MAPKs Fus3 and Kss1. These closely related kinases are activated by the common upstream MAPK kinase Ste7 yet generate distinct output responses, mating and filamentous growth, respectively. We find that docking interactions are necessary for communication with the kinases and that they can encode subtle differences in pathway-specific input and output. The cell cycle arrest mediator Far1, a mating-specific substrate, has a docking motif that selectively binds Fus3. In contrast, the shared partner Ste7 has a promiscuous motif that binds both Fus3 and Kss1. Structural analysis reveals that Fus3 interacts with specific and promiscuous peptides in conformationally distinct modes. Induced fit recognition may allow docking peptides to achieve discrimination by exploiting subtle differences in kinase flexibility.

The role of docking interactions in mediating signaling input, output, and discrimination in the yeast MAPK network.,Remenyi A, Good MC, Bhattacharyya RP, Lim WA Mol Cell. 2005 Dec 22;20(6):951-62. PMID:16364919^[5]

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

References

↑ Madhani HD, Styles CA, Fink GR. MAP kinases with distinct inhibitory functions impart signaling specificity during yeast differentiation. Cell. 1997 Nov 28;91(5):673-84. PMID:9393860
↑ Tedford K, Kim S, Sa D, Stevens K, Tyers M. Regulation of the mating pheromone and invasive growth responses in yeast by two MAP kinase substrates. Curr Biol. 1997 Apr 1;7(4):228-38. PMID:9094309
↑ Sabbagh W Jr, Flatauer LJ, Bardwell AJ, Bardwell L. Specificity of MAP kinase signaling in yeast differentiation involves transient versus sustained MAPK activation. Mol Cell. 2001 Sep;8(3):683-91. PMID:11583629
↑ Zeitlinger J, Simon I, Harbison CT, Hannett NM, Volkert TL, Fink GR, Young RA. Program-specific distribution of a transcription factor dependent on partner transcription factor and MAPK signaling. Cell. 2003 May 2;113(3):395-404. PMID:12732146
↑ Remenyi A, Good MC, Bhattacharyya RP, Lim WA. The role of docking interactions in mediating signaling input, output, and discrimination in the yeast MAPK network. Mol Cell. 2005 Dec 22;20(6):951-62. PMID:16364919 doi:http://dx.doi.org/10.1016/j.molcel.2005.10.030

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/2b9f"

@@ Line 1: / Line 1: @@
 ==Crystal structure of non-phosphorylated Fus3==
 <StructureSection load='2b9f' size='340' side='right' caption='[[2b9f]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FUS3, DAC2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b9f OCA], [http://pdbe.org/2b9f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2b9f RCSB], [http://www.ebi.ac.uk/pdbsum/2b9f PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b9f OCA], [http://pdbe.org/2b9f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2b9f RCSB], [http://www.ebi.ac.uk/pdbsum/2b9f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2b9f ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b9/2b9f_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b9/2b9f_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2b9f

From Proteopedia

Revision as of 06:32, 16 May 2018

Crystal structure of non-phosphorylated Fus3

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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