7dfu: Difference between revisions
New page: '''Unreleased structure''' The entry 7dfu is ON HOLD Authors: Yang, C.-G., Yang, T. Description: Crystal structure of Xanthomonas oryzae ClpP S68Y in complex with ADEP4. [[Category: Un... |
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==Crystal structure of Xanthomonas oryzae ClpP S68Y in complex with ADEP4.== | |||
<StructureSection load='7dfu' size='340' side='right'caption='[[7dfu]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7dfu]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_oryzae Xanthomonas oryzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DFU FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.901Å</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=EZA:N-[(6aS,12S,15aS,17R,21R,23aS)-17,21-dimethyl-6,11,15,20,23-pentaoxooctadecahydro-2H,6H,11H,15H-pyrido[2,1-i]dipyrrolo[2,1-c 2,1-l][1,4,7,10,13]oxatetraazacyclohexadecin-12-yl]-3,5-difluoro-Nalpha-[(2E)-hept-2-enoyl]-L-phenylalaninamide'>EZA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7dfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dfu OCA], [https://pdbe.org/7dfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dfu RCSB], [https://www.ebi.ac.uk/pdbsum/7dfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dfu ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CLPP_XANOR CLPP_XANOR] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.[HAMAP-Rule:MF_00444] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Rice bacterial leaf blight caused by Xanthomonas oryzae pv. oryzae (Xoo) is considered a destructive plant bacterial disease. The looming crisis of antibiotic resistance necessitates the discovery of antibiotics with new modes of action. Activated caseinolytic protease P (ClpP) can degrade bacterial FtsZ proteins that are essential for cell division; thus, we hypothesized that small-molecule-induced dysregulation of XooClpP may result in degradation of XooFtsZ to treat leaf blight diseases. In this work, we have determined the crystal structures of XooClpP, and its mutant bound with ADEP4, which revealed the action modes of XooClpP assemblies and XooFtsZ degradation by dysregulated XooClpP in the presence of small-molecule activators, such as ONC212 and ADEP4. Additionally, an antibacterial assessment demonstrated that ONC212 displays excellent activity against Xoo and prevents rice bacterial leaf blight in vivo. Thus, these unique antibacterial effects of small-molecule activators of XooClpP represent a potential strategy for the development of agricultural antibiotics by targeting bacterial ClpP. | |||
Dysregulation of ClpP by Small-Molecule Activators Used Against Xanthomonas oryzae pv. oryzae Infections.,Yang T, Zhang T, Zhou X, Wang P, Gan J, Song B, Yang S, Yang CG J Agric Food Chem. 2021 Jul 14;69(27):7545-7553. doi: 10.1021/acs.jafc.1c01470., Epub 2021 Jul 3. PMID:34218658<ref>PMID:34218658</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7dfu" style="background-color:#fffaf0;"></div> | ||
[[Category: Yang | |||
==See Also== | |||
*[[Clp protease 3D structures|Clp protease 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Xanthomonas oryzae]] | |||
[[Category: Yang C-G]] | |||
[[Category: Yang T]] | |||
Latest revision as of 19:32, 29 November 2023
Crystal structure of Xanthomonas oryzae ClpP S68Y in complex with ADEP4.Crystal structure of Xanthomonas oryzae ClpP S68Y in complex with ADEP4.
Structural highlights
FunctionCLPP_XANOR Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.[HAMAP-Rule:MF_00444] Publication Abstract from PubMedRice bacterial leaf blight caused by Xanthomonas oryzae pv. oryzae (Xoo) is considered a destructive plant bacterial disease. The looming crisis of antibiotic resistance necessitates the discovery of antibiotics with new modes of action. Activated caseinolytic protease P (ClpP) can degrade bacterial FtsZ proteins that are essential for cell division; thus, we hypothesized that small-molecule-induced dysregulation of XooClpP may result in degradation of XooFtsZ to treat leaf blight diseases. In this work, we have determined the crystal structures of XooClpP, and its mutant bound with ADEP4, which revealed the action modes of XooClpP assemblies and XooFtsZ degradation by dysregulated XooClpP in the presence of small-molecule activators, such as ONC212 and ADEP4. Additionally, an antibacterial assessment demonstrated that ONC212 displays excellent activity against Xoo and prevents rice bacterial leaf blight in vivo. Thus, these unique antibacterial effects of small-molecule activators of XooClpP represent a potential strategy for the development of agricultural antibiotics by targeting bacterial ClpP. Dysregulation of ClpP by Small-Molecule Activators Used Against Xanthomonas oryzae pv. oryzae Infections.,Yang T, Zhang T, Zhou X, Wang P, Gan J, Song B, Yang S, Yang CG J Agric Food Chem. 2021 Jul 14;69(27):7545-7553. doi: 10.1021/acs.jafc.1c01470., Epub 2021 Jul 3. PMID:34218658[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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