4ka7: Difference between revisions

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'''Unreleased structure'''


The entry 4ka7 is ON HOLD
==Structure of Organellar OligoPeptidase (E572Q) in complex with an endogenous substrate==
 
<StructureSection load='4ka7' size='340' side='right'caption='[[4ka7]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
Authors: Berntsson, R.P-A., Kmiec, B., Teixeira, P.F., Svensson, L.M., Bakali, A., Glaser, E., Stenmark, P.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[4ka7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KA7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KA7 FirstGlance]. <br>
Description: Structure of Organellar OligoPeptidase (E572Q) in complex with an endogenous substrate
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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=4ka7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ka7 OCA], [https://pdbe.org/4ka7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ka7 RCSB], [https://www.ebi.ac.uk/pdbsum/4ka7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ka7 ProSAT]</span></td></tr>
</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>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Bakali A]]
[[Category: Berntsson RP-A]]
[[Category: Glaser E]]
[[Category: Kmiec B]]
[[Category: Stenmark P]]
[[Category: Svensson LM]]
[[Category: Teixeira PF]]

Latest revision as of 11:54, 20 March 2024

Structure of Organellar OligoPeptidase (E572Q) in complex with an endogenous substrateStructure of Organellar OligoPeptidase (E572Q) in complex with an endogenous substrate

Structural highlights

4ka7 is a 2 chain structure with sequence from Arabidopsis thaliana and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2]

References

  1. ↑ Moreau M, Westlake T, Zampogna G, Popescu G, Tian M, Noutsos C, Popescu S. The Arabidopsis oligopeptidases TOP1 and TOP2 are salicylic acid targets that modulate SA-mediated signaling and the immune response. Plant J. 2013 Nov;76(4):603-14. doi: 10.1111/tpj.12320. Epub 2013 Oct 18. PMID:24004003 doi:http://dx.doi.org/10.1111/tpj.12320
  2. ↑ 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. Organellar oligopeptidase (OOP) provides a complementary pathway for targeting peptide degradation in mitochondria and chloroplasts. 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 doi:http://dx.doi.org/10.1073/pnas.1307637110

4ka7, resolution 1.80Å

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