View source for 6o60


==Crystal structure of GGTase3-FBXL2-SKP1 complex==
<StructureSection load='6o60' size='340' side='right'caption='[[6o60]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6o60]] is a 4 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=6O60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O60 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]] 2.503&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=6o60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o60 OCA], [https://pdbe.org/6o60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o60 RCSB], [https://www.ebi.ac.uk/pdbsum/6o60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o60 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PTAR1_HUMAN PTAR1_HUMAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Protein prenylation is believed to be catalyzed by three heterodimeric enzymes: FTase, GGTase1 and GGTase2. Here we report the identification of a previously unknown human prenyltransferase complex consisting of an orphan prenyltransferase alpha-subunit, PTAR1, and the catalytic beta-subunit of GGTase2, RabGGTB. This enzyme, which we named GGTase3, geranylgeranylates FBXL2 to allow its localization at cell membranes, where this ubiquitin ligase mediates the polyubiquitylation of membrane-anchored proteins. In cells, FBXL2 is specifically recognized by GGTase3 despite having a typical carboxy-terminal CaaX prenylation motif that is predicted to be recognized by GGTase1. Our crystal structure analysis of the full-length GGTase3-FBXL2-SKP1 complex reveals an extensive multivalent interface specifically formed between the leucine-rich repeat domain of FBXL2 and PTAR1, which unmasks the structural basis of the substrate-enzyme specificity. By uncovering a missing prenyltransferase and its unique mode of substrate recognition, our findings call for a revision of the 'prenylation code'.

GGTase3 is a newly identified geranylgeranyltransferase targeting a ubiquitin ligase.,Kuchay S, Wang H, Marzio A, Jain K, Homer H, Fehrenbacher N, Philips MR, Zheng N, Pagano M Nat Struct Mol Biol. 2019 Jul;26(7):628-636. doi: 10.1038/s41594-019-0249-3. Epub, 2019 Jun 17. PMID:31209342<ref>PMID:31209342</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6o60" style="background-color:#fffaf0;"></div>

==See Also==
*[[Geranylgeranyl transferase 3D structures|Geranylgeranyl transferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Wang H]]
[[Category: Zheng N]]