This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1a4o

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1a4o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a4o, resolution 2.8&Aring;" /> '''14-3-3 PROTEIN ZETA I...)
Current revision (06:27, 7 February 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1a4o.gif|left|200px]]<br /><applet load="1a4o" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1a4o, resolution 2.8&Aring;" />
 
-
'''14-3-3 PROTEIN ZETA ISOFORM'''<br />
 
-
==Overview==
+
==14-3-3 PROTEIN ZETA ISOFORM==
-
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.
+
<StructureSection load='1a4o' size='340' side='right'caption='[[1a4o]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 +
== Structural highlights ==
 +
<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>
 +
</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>
 +
<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>
 +
</table>
 +
== Function ==
 +
[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>
-
==About this Structure==
+
==See Also==
-
1A4O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A4O OCA].
+
*[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=7603574 7603574]
+
__TOC__
 +
</StructureSection>
[[Category: Bos taurus]]
[[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://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:36:26 2007''
+

Current revision

14-3-3 PROTEIN ZETA ISOFORM

PDB ID 1a4o

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools