8w6v
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Structural basis of chorismate isomerization by Arabidopsis isochorismate synthase ICS1== | |
| + | <StructureSection load='8w6v' size='340' side='right'caption='[[8w6v]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8w6v]] is a 2 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=8W6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8W6V 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]] 1.8Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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=8w6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8w6v OCA], [https://pdbe.org/8w6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8w6v RCSB], [https://www.ebi.ac.uk/pdbsum/8w6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8w6v ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ICS1_ARATH ICS1_ARATH] Isochorismate synthase involved in the synthesis of salicylic acid (SA) required for both local and systemic acquired resistance (LAR and SAR) while SA synthesized through the phenylalanine ammonium lyase (PAL) pathway seems to potentiate plant cell death. Also involved in phylloquinone (vitamin K1) synthesis. Has no isochorismate pyruvate lyase (IPL) activity.<ref>PMID:10449575</ref> <ref>PMID:11734859</ref> <ref>PMID:16617180</ref> <ref>PMID:17190832</ref> <ref>PMID:18451262</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Salicylic acid (SA) plays a crucial role in plant defense against biotrophic and semi-biotrophic pathogens. In Arabidopsis (Arabidopsis thaliana), isochorismate synthase 1 (AtICS1) is a key enzyme for the pathogen-induced biosynthesis of SA via catalytic conversion of chorismate into isochorismate, an essential precursor for SA synthesis. Despite the extensive knowledge of ICS1-related menaquinone, siderophore, tryptophan (MST) enzymes in bacteria, the structural mechanisms for substrate binding and catalysis in plant isochorismate synthase (ICS) enzymes are unknown. This study reveals that plant ICS enzymes catalyze the isomerization of chorismate through a magnesium-dependent mechanism, with AtICS1 exhibiting the most substantial catalytic activity. Additionally, we present high-resolution crystal structures of apo AtICS1 and its complex with chorismate, offering detailed insights into the mechanisms of substrate recognition and catalysis. Importantly, our investigation indicates the existence of a potential substrate entrance channel and a gating mechanism regulating substrate into the catalytic site. Structural comparisons of AtICS1 with MST enzymes suggest a shared structural framework with conserved gating and catalytic mechanisms. This work provides valuable insights into the structural and regulatory mechanisms governing substrate delivery and catalysis in AtICS1, as well as other plant ICS enzymes. | ||
| - | + | Structural basis of chorismate isomerization by Arabidopsis ISOCHORISMATE SYNTHASE1.,Su Z, Niu C, Zhou S, Xu G, Zhu P, Fu Q, Zhang Y, Ming Z Plant Physiol. 2024 May 3:kiae260. doi: 10.1093/plphys/kiae260. PMID:38701037<ref>PMID:38701037</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8w6v" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Arabidopsis thaliana]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ming ZH]] | ||
| + | [[Category: Su ZH]] | ||
Revision as of 08:06, 22 May 2024
Structural basis of chorismate isomerization by Arabidopsis isochorismate synthase ICS1
| |||||||||||
