View source for 4dk3


==Structure of Editosome protein==
<StructureSection load='4dk3' size='340' side='right'caption='[[4dk3]], [[Resolution|resolution]] 2.76&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4dk3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lama_glama Lama glama] and [https://en.wikipedia.org/wiki/Trypanosoma_brucei Trypanosoma brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DK3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DK3 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]] 2.76&#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=4dk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dk3 OCA], [https://pdbe.org/4dk3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dk3 RCSB], [https://www.ebi.ac.uk/pdbsum/4dk3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dk3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q95W15_9TRYP Q95W15_9TRYP] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Trypanosomatids, such as the sleeping sickness parasite Trypanosoma brucei, contain a approximately 20S RNA-editing complex, also called the editosome, which is required for U-insertion/deletion editing of mitochondrial mRNAs. The editosome contains a core of 12 proteins including the large interaction protein A1, the small interaction protein A6, and the editing RNA ligase L2. Using biochemical and structural data, we identified distinct domains of T. brucei A1 which specifically recognize A6 and L2. We provide evidence that an N-terminal domain of A1 interacts with the C-terminal domain of L2. The C-terminal domain of A1 appears to be required for the interaction with A6 and also plays a key role in RNA binding by the RNA-editing ligase L2 in trans. Three crystal structures of the C-terminal domain of A1 have been elucidated, each in complex with a nanobody as a crystallization chaperone. These structures permitted the identification of putative dsRNA recognition sites. Mutational analysis of conserved residues of the C-terminal domain identified Arg703, Arg731 and Arg734 as key requirements for RNA binding. The data show that the editing RNA ligase activity is modulated by a novel mechanism, i.e. by the trans-acting RNA binding C-terminal domain of A1.

The structure of the C-terminal domain of the largest editosome interaction protein and its role in promoting RNA binding by RNA-editing ligase L2.,Park YJ, Budiarto T, Wu M, Pardon E, Steyaert J, Hol WG Nucleic Acids Res. 2012 May 4. PMID:22561373<ref>PMID:22561373</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4dk3" style="background-color:#fffaf0;"></div>

==See Also==
*[[Antibody 3D structures|Antibody 3D structures]]
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Lama glama]]
[[Category: Large Structures]]
[[Category: Trypanosoma brucei]]
[[Category: Hol W]]
[[Category: Park Y-J]]