4ka8: Difference between revisions
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<StructureSection load='4ka8' size='340' side='right'caption='[[4ka8]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='4ka8' size='340' side='right'caption='[[4ka8]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ka8]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ka8]] is a 1 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=4KA8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KA8 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <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=4ka8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ka8 OCA], [https://pdbe.org/4ka8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ka8 RCSB], [https://www.ebi.ac.uk/pdbsum/4ka8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ka8 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/OOPDA_ARATH OOPDA_ARATH] Oligopeptidase degrading short peptides from 8 to 23 amino acid residues. Plays a role in the degradation of transit peptides and of peptides derived from other proteolytic events. Does not exhibit a strict cleavage pattern. Binds salicylic acid.<ref>PMID:24004003</ref> <ref>PMID:24043784</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Arabidopsis thaliana]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bakali | [[Category: Bakali A]] | ||
[[Category: Berntsson | [[Category: Berntsson RP-A]] | ||
[[Category: Glaser | [[Category: Glaser E]] | ||
[[Category: Kmiec | [[Category: Kmiec B]] | ||
[[Category: Stenmark | [[Category: Stenmark P]] | ||
[[Category: Svensson | [[Category: Svensson LM]] | ||
[[Category: Teixeira | [[Category: Teixeira PF]] | ||
Revision as of 14:48, 30 November 2022
Structure of Organellar OligoPeptidaseStructure of Organellar OligoPeptidase
Structural highlights
FunctionOOPDA_ARATH Oligopeptidase degrading short peptides from 8 to 23 amino acid residues. Plays a role in the degradation of transit peptides and of peptides derived from other proteolytic events. Does not exhibit a strict cleavage pattern. Binds salicylic acid.[1] [2] Publication Abstract from PubMedBoth mitochondria and chloroplasts contain distinct proteolytic systems for precursor protein processing catalyzed by the mitochondrial and stromal processing peptidases and for the degradation of targeting peptides catalyzed by presequence protease. Here, we have identified and characterized a component of the organellar proteolytic systems in Arabidopsis thaliana, the organellar oligopeptidase, OOP (At5g65620). OOP belongs to the M3A family of peptide-degrading metalloproteases. Using two independent in vivo methods, we show that the protease is dually localized to mitochondria and chloroplasts. Furthermore, we localized the OPP homolog At5g10540 to the cytosol. Analysis of peptide degradation by OOP revealed substrate size restriction from 8 to 23 aa residues. Short mitochondrial targeting peptides (presequence of the ribosomal protein L29 and presequence of 1-aminocyclopropane-1-carboxylic acid deaminase 1) and N- and C-terminal fragments derived from the presequence of the ATPase beta subunit ranging in size from 11 to 20 aa could be degraded. MS analysis showed that OOP does not exhibit a strict cleavage pattern but shows a weak preference for hydrophobic residues (F/L) at the P1 position. The crystal structures of OOP, at 1.8-1.9 A, exhibit an ellipsoidal shape consisting of two major domains enclosing the catalytic cavity of 3,000 A(3). The structural and biochemical data suggest that the protein undergoes conformational changes to allow peptide binding and proteolysis. Our results demonstrate the complementary role of OOP in targeting-peptide degradation in mitochondria and chloroplasts. Organellar oligopeptidase (OOP) provides a complementary pathway for targeting peptide degradation in mitochondria and chloroplasts.,Kmiec B, Teixeira PF, Berntsson RP, Murcha MW, Branca RM, Radomiljac JD, Regberg J, Svensson LM, Bakali A, Langel U, Lehtio J, Whelan J, Stenmark P, Glaser E Proc Natl Acad Sci U S A. 2013 Oct 1;110(40):E3761-9. doi:, 10.1073/pnas.1307637110. Epub 2013 Sep 16. PMID:24043784[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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