View source for 3wso


==Crystal structure of the Skp1-FBG3 complex==
<StructureSection load='3wso' size='340' side='right'caption='[[3wso]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wso]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WSO 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]] 2.6&#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=3wso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wso OCA], [https://pdbe.org/3wso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wso RCSB], [https://www.ebi.ac.uk/pdbsum/3wso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wso ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FBX44_HUMAN FBX44_HUMAN] Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Skp1-Cul1-F-box protein (SCF) complex catalyzes protein ubiquitination in diverse cellular processes and is one of the best-characterized ubiquitin ligases. F-box proteins determine the substrate specificities of SCF ubiquitin ligases. Among these, Fbs1/FBG1/FBXO2, Fbs2/FBG2/FBXO6, and Fbs3/FBG5/FBXO27 recognize the N-glycans of glycoproteins, whereas FBG3/FBXO44 has no sugar-binding activity, despite the high sequence homology and conservation of the residues necessary for oligosaccharide binding between Fbs1-3 and FBG3. Here we determined the crystal structure of the Skp1-FBG3 complex at a resolution of 2.6 A. The substrate-binding domain of FBG3 is composed of a 10-stranded antiparallel beta-sandwich with three helices. Although the overall structure of FBG3 is similar to that of Fbs1, the residues that form the Fbs1 carbohydrate-binding pocket failed to be superposed with the corresponding residues of FBG3. Structure-based mutational analysis shows that distinct hydrogen bond networks of four FBG3 loops, i.e., beta2-beta3, beta5-beta6, beta7-beta8, and beta9-beta10, prevent the formation of the carbohydrate-binding pocket shown in Fbs1.

The Structural Differences between a Glycoprotein Specific F-Box Protein Fbs1 and Its Homologous Protein FBG3.,Kumanomidou T, Nishio K, Takagi K, Nakagawa T, Suzuki A, Yamane T, Tokunaga F, Iwai K, Murakami A, Yoshida Y, Tanaka K, Mizushima T PLoS One. 2015 Oct 13;10(10):e0140366. doi: 10.1371/journal.pone.0140366., eCollection 2015. PMID:26460611<ref>PMID:26460611</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wso" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Iwai K]]
[[Category: Kumanomidou T]]
[[Category: Mizushima T]]
[[Category: Murakami A]]
[[Category: Nakagawa T]]
[[Category: Nishio K]]
[[Category: Suzuki A]]
[[Category: Takagi K]]
[[Category: Tanaka K]]
[[Category: Tokunaga F]]
[[Category: Yamane T]]
[[Category: Yoshida Y]]