7o4f: Difference between revisions

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<StructureSection load='7o4f' size='340' side='right'caption='[[7o4f]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
<StructureSection load='7o4f' size='340' side='right'caption='[[7o4f]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7o4f]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O4F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O4F FirstGlance]. <br>
<table><tr><td colspan='2'>[[7o4f]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O4F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O4F FirstGlance]. <br>
</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7o4e|7o4e]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PCMP-H83, OTP86, At3g63370, F16M2_220 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=7o4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o4f OCA], [https://pdbe.org/7o4f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o4f RCSB], [https://www.ebi.ac.uk/pdbsum/7o4f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o4f ProSAT]</span></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=7o4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o4f OCA], [https://pdbe.org/7o4f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o4f RCSB], [https://www.ebi.ac.uk/pdbsum/7o4f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o4f ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/PP296_ARATH PP296_ARATH]] Involved in RNA editing event in chloroplasts. Required for the editing of a single site in rps14 transcript.<ref>PMID:19934379</ref> 
[https://www.uniprot.org/uniprot/PP296_ARATH PP296_ARATH] Involved in RNA editing event in chloroplasts. Required for the editing of a single site in rps14 transcript.<ref>PMID:19934379</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
RNA editosomes selectively deaminate cytidines to uridines in plant organellar transcripts-mostly to restore protein functionality and consequently facilitate mitochondrial and chloroplast function. The RNA editosomal pentatricopeptide repeat proteins serve target RNA recognition, whereas the intensively studied DYW domain elicits catalysis. Here we present structures and functional data of a DYW domain in an inactive ground state and activated. DYW domains harbour a cytidine deaminase fold and a C-terminal DYW motif, with catalytic and structural zinc atoms, respectively. A conserved gating domain within the deaminase fold regulates the active site sterically and mechanistically in a process that we termed gated zinc shutter. Based on the structures, an autoinhibited ground state and its activation are cross-validated by RNA editing assays and differential scanning fluorimetry. We anticipate that, in vivo, the framework of an active plant RNA editosome triggers the release of DYW autoinhibition to ensure a controlled and coordinated cytidine deamination playing a key role in mitochondrial and chloroplast homeostasis.
 
DYW domain structures imply an unusual regulation principle in plant organellar RNA editing catalysis.,Takenaka M, Takenaka S, Barthel T, Frink B, Haag S, Verbitskiy D, Oldenkott B, Schallenberg-Rudinger M, Feiler CG, Weiss MS, Palm GJ, Weber G Nat Catal. 2021 Jun;4(6):510-522. doi: 10.1038/s41929-021-00633-x. Epub 2021 Jun , 21. PMID:34712911<ref>PMID:34712911</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7o4f" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Arath]]
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Barthel, T]]
[[Category: Barthel T]]
[[Category: Feiler, C]]
[[Category: Feiler C]]
[[Category: Palm, G J]]
[[Category: Palm GJ]]
[[Category: Takenaka, M]]
[[Category: Takenaka M]]
[[Category: Weber, G]]
[[Category: Weber G]]
[[Category: Weiss, M S]]
[[Category: Weiss MS]]
[[Category: Cytidine deaminase]]
[[Category: Hydrolase]]

Latest revision as of 07:50, 1 May 2024

The DYW domain of A. thaliana OTP86 in its active state

7o4f, resolution 1.65Å

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