2p63

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:24, 6 November 2024) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2p63.jpg|left|200px]]
 
-
{{Structure
+
==Suprafacial orientation of the SCFCdc4 dimer accommodates multiple geometries for substrate ubiquitination==
-
|PDB= 2p63 |SIZE=350|CAPTION= <scene name='initialview01'>2p63</scene>, resolution 2.67&Aring;
+
<StructureSection load='2p63' size='340' side='right'caption='[[2p63]], [[Resolution|resolution]] 2.67&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
+
<table><tr><td colspan='2'>[[2p63]] is a 4 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=2P63 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P63 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]] 2.67&#8491;</td></tr>
-
|GENE= CDC4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-
|DOMAIN=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2p63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p63 OCA], [https://pdbe.org/2p63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p63 RCSB], [https://www.ebi.ac.uk/pdbsum/2p63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p63 ProSAT]</span></td></tr>
-
|RELATEDENTRY=
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2p63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p63 OCA], [http://www.ebi.ac.uk/pdbsum/2p63 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2p63 RCSB]</span>
+
== Function ==
-
}}
+
[https://www.uniprot.org/uniprot/CDC4_YEAST CDC4_YEAST] Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes and binds to phosphorylated target proteins. Directs ubiquitination of the phosphorylated CDK inhibitor SIC1. Involved in the degradation of CDC6 together with CDC34/UBC3 and CDC53, and in restricting the degradation of FAR1 to the nucleus. Is essential for initiation of DNA replication and separation of the spindle pole bodies to form the poles of the mitotic spindle. It also plays a role in bud development, fusion of zygotic nuclei after conjugation and various aspects of sporulation. Required for HTA1-HTB1 locus transcription activation. Required for G1/S and G2/M transition.<ref>PMID:7813440</ref> <ref>PMID:9346238</ref> <ref>PMID:9346239</ref> <ref>PMID:9312022</ref> <ref>PMID:9312054</ref> <ref>PMID:9736614</ref> <ref>PMID:10409741</ref> <ref>PMID:10213692</ref> <ref>PMID:11080155</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
SCF ubiquitin ligases recruit substrates for degradation via F box protein adaptor subunits. WD40 repeat F box proteins, such as Cdc4 and beta-TrCP, contain a conserved dimerization motif called the D domain. Here, we report that the D domain protomers of yeast Cdc4 and human beta-TrCP form a superhelical homotypic dimer. Disruption of the D domain compromises the activity of yeast SCF(Cdc4) toward the CDK inhibitor Sic1 and other substrates. SCF(Cdc4) dimerization has little effect on the affinity for Sic1 but markedly stimulates ubiquitin conjugation. A model of the dimeric holo-SCF(Cdc4) complex based on small-angle X-ray scatter measurements reveals a suprafacial configuration, in which substrate-binding sites and E2 catalytic sites lie in the same plane with a separation of 64 A within and 102 A between each SCF monomer. This spatial variability may accommodate diverse acceptor lysine geometries in both substrates and the elongating ubiquitin chain and thereby increase catalytic efficiency.
-
'''Suprafacial orientation of the SCFCdc4 dimer accommodates multiple geometries for substrate ubiquitination'''
+
Suprafacial orientation of the SCFCdc4 dimer accommodates multiple geometries for substrate ubiquitination.,Tang X, Orlicky S, Lin Z, Willems A, Neculai D, Ceccarelli D, Mercurio F, Shilton BH, Sicheri F, Tyers M Cell. 2007 Jun 15;129(6):1165-76. PMID:17574027<ref>PMID:17574027</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
==About this Structure==
+
</div>
-
2P63 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=2P63 OCA].
+
<div class="pdbe-citations 2p63" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
-
[[Category: Single protein]]
+
[[Category: Ceccarelli D]]
-
[[Category: Ceccarelli, D.]]
+
[[Category: Neculai D]]
-
[[Category: Neculai, D.]]
+
[[Category: Orlicky S]]
-
[[Category: Orlicky, S.]]
+
-
[[Category: helix bundle]]
+
-
[[Category: scf complex]]
+
-
[[Category: ubiquitination]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:30:26 2008''
+

Current revision

Suprafacial orientation of the SCFCdc4 dimer accommodates multiple geometries for substrate ubiquitination

PDB ID 2p63

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2p63"
Personal tools