5ydg: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 3: Line 3:
<StructureSection load='5ydg' size='340' side='right' caption='[[5ydg]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
<StructureSection load='5ydg' size='340' side='right' caption='[[5ydg]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5ydg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YDG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YDG FirstGlance]. <br>
<table><tr><td colspan='2'>[[5ydg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YDG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YDG FirstGlance]. <br>
</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=5ydg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ydg OCA], [http://pdbe.org/5ydg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ydg RCSB], [http://www.ebi.ac.uk/pdbsum/5ydg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ydg ProSAT]</span></td></tr>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MORF2, DAL1, RIP2, At2g33430 ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ydg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ydg OCA], [http://pdbe.org/5ydg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ydg RCSB], [http://www.ebi.ac.uk/pdbsum/5ydg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ydg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/MORF2_ARATH MORF2_ARATH]] Involved in plastid rRNA processing and consequently in translation and early chloroplast differentiation (PubMed:12678554). Involved in organellar RNA editing. Required for the processing of multiple editing sites in plastids (PubMed:22411807, PubMed:23818871).<ref>PMID:12678554</ref> <ref>PMID:22411807</ref> <ref>PMID:23818871</ref>   
[[http://www.uniprot.org/uniprot/MORF2_ARATH MORF2_ARATH]] Involved in plastid rRNA processing and consequently in translation and early chloroplast differentiation (PubMed:12678554). Involved in organellar RNA editing. Required for the processing of multiple editing sites in plastids (PubMed:22411807, PubMed:23818871).<ref>PMID:12678554</ref> <ref>PMID:22411807</ref> <ref>PMID:23818871</ref>   
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
RNA editing is a post-transcription process that alters the genetic information on RNA molecules. In plastids and mitochondria of flowering plants, the multiple organellar RNA editing factors (MORFs) interact with the PLS-type pentatricopeptide repeat (PPR) proteins and participate in RNA editing of cytidine-to-uridine conversion. The PPR proteins recognize cytidine targets around the editing sites, and the MORF proteins modulate the RNA-binding activity of the PPR proteins. Here, we report the structure of the Arabidopsis thaliana chloroplast MORF2 at 2.4 A resolution. The structure, adopting typical MORF-box fold as observed in mitochondrial MORF1 and chloroplast MORF9, reveals an MORF1-like dimerization mode. The difference between the two dimerization modes can be attributed to F157 (corresponding F162 in MORF1 and W160 in MORF9), which causes a 60 degrees shift upon dimerization. This observation, together with the PPR-MORF2 model, suggests a dimer-to-monomer transition during RNA editosome formation.
Crystal structure of the chloroplast RNA editing factor MORF2.,Yang J, Zhang M, Wang X Biochem Biophys Res Commun. 2017 Dec 8. pii: S0006-291X(17)32435-X. doi:, 10.1016/j.bbrc.2017.12.044. PMID:29229384<ref>PMID:29229384</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ydg" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Arath]]
[[Category: Gao, Y S]]
[[Category: Gao, Y S]]
[[Category: Wang, X]]
[[Category: Wang, X]]