View source for 4dk6


==Structure of Editosome protein==
<StructureSection load='4dk6' size='340' side='right'caption='[[4dk6]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4dk6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Camelus_glama Camelus glama] and [http://en.wikipedia.org/wiki/Trypanosoma_(trypanozoon)_brucei Trypanosoma (trypanozoon) brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DK6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DK6 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4dk3|4dk3]], [[4dka|4dka]]</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4dk6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dk6 OCA], [http://pdbe.org/4dk6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dk6 RCSB], [http://www.ebi.ac.uk/pdbsum/4dk6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dk6 ProSAT]</span></td></tr>
</table>
<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 4dk6" style="background-color:#fffaf0;"></div>

==See Also==
*[[Antibody 3D structures|Antibody 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Camelus glama]]
[[Category: Large Structures]]
[[Category: Hol, W]]
[[Category: Park, Y J]]
[[Category: Krepa1]]
[[Category: Protein binding]]
[[Category: Rna binding protein-immune system complex]]
[[Category: Single domain antibody]]
[[Category: Vhh]]