4ppu: Difference between revisions
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<StructureSection load='4ppu' size='340' side='right'caption='[[4ppu]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='4ppu' size='340' side='right'caption='[[4ppu]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ppu]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ppu]] 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=4PPU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PPU FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TYR:TYROSINE'>TYR</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ppu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ppu OCA], [https://pdbe.org/4ppu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ppu RCSB], [https://www.ebi.ac.uk/pdbsum/4ppu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ppu ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/CM1_ARATH CM1_ARATH] May play a role in chloroplast biogenesis (Potential). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 21: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 4ppu" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4ppu" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[3D structures of chorismate mutase|3D structures of chorismate mutase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Arabidopsis thaliana]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Jez | [[Category: Jez JM]] | ||
[[Category: Westfall | [[Category: Westfall CS]] | ||
[[Category: Xu | [[Category: Xu A]] | ||
Latest revision as of 20:20, 20 September 2023
Crystal Structure of AtCM1 with Tyrosine Bound in Allosteric SiteCrystal Structure of AtCM1 with Tyrosine Bound in Allosteric Site
Structural highlights
FunctionCM1_ARATH May play a role in chloroplast biogenesis (Potential). Publication Abstract from PubMedChorismate mutase converts chorismate into prephenate for aromatic amino acid biosynthesis. To understand the molecular basis of allosteric regulation in the plant chorismate mutases, we analyzed the three Arabidopsis thaliana chorismate mutase isoforms (AtCM1-3) and determined the x-ray crystal structures of AtCM1 in complex with phenylalanine and tyrosine. Functional analyses show a wider range of effector control in the Arabidopsis chorismate mutases than previously reported. AtCM1 is activated by tryptophan with phenylalanine and tyrosine acting as negative effectors; however, tryptophan, cysteine, and histidine activate AtCM3. AtCM2 is a nonallosteric form. The crystal structure of AtCM1 in complex with tyrosine and phenylalanine identifies differences in the effector sites of the allosterically regulated yeast enzyme and the other two Arabidopsis isoforms. Site-directed mutagenesis of residues in the effector site reveals key features leading to differential effector regulation in these enzymes. In AtCM1, mutations of Gly-213 abolish allosteric regulation, as observed in AtCM2. A second effector site position, Gly-149 in AtCM1 and Asp-132 in AtCM3, controls amino acid effector specificity in AtCM1 and AtCM3. Comparisons of chorismate mutases from multiple plants suggest that subtle differences in the effector site are conserved in different lineages and may lead to specialized regulation of this branch point enzyme. Structural evolution of differential amino Acid effector regulation in plant chorismate mutases.,Westfall CS, Xu A, Jez JM J Biol Chem. 2014 Oct 10;289(41):28619-28. doi: 10.1074/jbc.M114.591123. Epub, 2014 Aug 26. PMID:25160622[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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