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| | <StructureSection load='4ppv' size='340' side='right'caption='[[4ppv]], [[Resolution|resolution]] 2.45Å' scene=''> | | <StructureSection load='4ppv' size='340' side='right'caption='[[4ppv]], [[Resolution|resolution]] 2.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ppv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PPV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PPV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ppv]] 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=4PPV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PPV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ppu|4ppu]]</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=4ppv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ppv OCA], [https://pdbe.org/4ppv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ppv RCSB], [https://www.ebi.ac.uk/pdbsum/4ppv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ppv ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CM1, At3g29200, MXO21.4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ppv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ppv OCA], [http://pdbe.org/4ppv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ppv RCSB], [http://www.ebi.ac.uk/pdbsum/4ppv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ppv ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CM1_ARATH CM1_ARATH]] May play a role in chloroplast biogenesis (Potential). | + | [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 == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4ppv" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4ppv" 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: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Chorismate mutase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jez, J M]] | + | [[Category: Jez JM]] |
| - | [[Category: Westfall, C S]] | + | [[Category: Westfall CS]] |
| - | [[Category: Xu, A]] | + | [[Category: Xu A]] |
| - | [[Category: Chorismate mutase ii]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Mutase]]
| + | |
| Structural highlights
Function
CM1_ARATH May play a role in chloroplast biogenesis (Potential).
Publication Abstract from PubMed
Chorismate 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 Also
References
- ↑ Westfall CS, Xu A, Jez JM. Structural evolution of differential amino Acid effector regulation in plant chorismate mutases. J Biol Chem. 2014 Oct 10;289(41):28619-28. doi: 10.1074/jbc.M114.591123. Epub, 2014 Aug 26. PMID:25160622 doi:http://dx.doi.org/10.1074/jbc.M114.591123
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