1a4o: Difference between revisions

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-[[Image:1a4o.gif|left|200px]]
- {{Structure
+==14-3-3 PROTEIN ZETA ISOFORM==
-|PDB= 1a4o |SIZE=350|CAPTION= <scene name='initialview01'>1a4o</scene>, resolution 2.8&Aring;
+<StructureSection load='1a4o' size='340' side='right'caption='[[1a4o]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND=
+<table><tr><td colspan='2'>[[1a4o]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A4O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A4O FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
-|GENE=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a4o OCA], [https://pdbe.org/1a4o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a4o RCSB], [https://www.ebi.ac.uk/pdbsum/1a4o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a4o ProSAT]</span></td></tr>
-|DOMAIN=
+</table>
-|RELATEDENTRY=
+== Function ==
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a4o OCA], [http://www.ebi.ac.uk/pdbsum/1a4o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a4o RCSB]</span>
+[https://www.uniprot.org/uniprot/1433Z_BOVIN 1433Z_BOVIN] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Activates the ADP-ribosyltransferase (exoS) activity of bacterial origin.<ref>PMID:7931346</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/a4/1a4o_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=1a4o ConSurf].
+<div style="clear:both"></div>
-'''14-3-3 PROTEIN ZETA ISOFORM'''
+==See Also==
+*[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]]
+== References ==
-==Overview==
+<references/>
-The 14-3-3 family of proteins have recently been identified as regulatory elements in intracellular signalling pathways: 14-3-3 proteins bind to oncogene and proto-oncogene products, including c-Raf-1 (refs 2-5), c-Bcr (ref. 6) and polyomavirus middle-T antigen; overexpression of 14-3-3 activates Raf kinase in yeast and induces meiotic maturation in Xenopus oocytes. Here we report the crystal structure of the major isoform of mammalian 14-3-3 proteins at 2.9 A resolution. Each subunit of the dimeric protein consists of a bundle of nine antiparallel helices that form a palisade around an amphipathic groove. The groove is large enough to accommodate a tenth helix, and we propose that binding to an amphipathic helix represents a general mechanism for the interaction of 14-3-3 with diverse cellular proteins. The residues in the dimer interface and the putative ligand-binding surface are invariant among vertebrates, yeast and plants, suggesting a conservation of structure and function throughout the 14-3-3 family.
+__TOC__
+</StructureSection>
-==About this Structure==
-A4O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A4O OCA].
-==Reference==
-Crystal structure of the zeta isoform of the 14-3-3 protein., Liu D, Bienkowska J, Petosa C, Collier RJ, Fu H, Liddington R, Nature. 1995 Jul 13;376(6536):191-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7603574 7603574]
 [[Category: Bos taurus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Bienkowska, J.]]
+[[Category: Bienkowska J]]
-[[Category: Collier, R J.]]
+[[Category: Collier RJ]]
-[[Category: Fu, H.]]
+[[Category: Fu H]]
-[[Category: Liddington, R C.]]
+[[Category: Liddington RC]]
-[[Category: Liu, D.]]
+[[Category: Liu D]]
-[[Category: Petosa, C.]]
+[[Category: Petosa C]]
-[[Category: signal transduction]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:33:10 2008''