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| | ==Physcomitrella patens Chorismate Mutase== | | ==Physcomitrella patens Chorismate Mutase== |
| - | <StructureSection load='5w6y' size='340' side='right' caption='[[5w6y]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='5w6y' size='340' side='right'caption='[[5w6y]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5w6y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Moss Moss]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W6Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5W6Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5w6y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Physcomitrium_patens Physcomitrium patens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W6Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5W6Y FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.995Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PHYPADRAFT_181106 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3218 Moss])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=5w6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w6y OCA], [https://pdbe.org/5w6y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5w6y RCSB], [https://www.ebi.ac.uk/pdbsum/5w6y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5w6y ProSAT]</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=5w6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w6y OCA], [http://pdbe.org/5w6y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5w6y RCSB], [http://www.ebi.ac.uk/pdbsum/5w6y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5w6y ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A9S498_PHYPA A9S498_PHYPA] |
| | <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 5w6y" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5w6y" 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: Chorismate mutase]] | + | [[Category: Large Structures]] |
| - | [[Category: Moss]] | + | [[Category: Physcomitrium patens]] |
| - | [[Category: Holland, C K]] | + | [[Category: Holland CK]] |
| - | [[Category: Jez, J M]] | + | [[Category: Jez JM]] |
| - | [[Category: Kroll, K]] | + | [[Category: Kroll K]] |
| - | [[Category: Biosynthetic protein]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| Structural highlights
Function
A9S498_PHYPA
Publication Abstract from PubMed
Plants, fungi, and bacteria synthesize the aromatic amino acids: L -phenylalanine, L -tyrosine, and L -tryptophan. Chorismate mutase catalyzes the branch point reaction of phenylalanine and tyrosine biosynthesis to generate prephenate. In Arabidopsis thaliana , there are two plastid-localized chorismate mutases that are allosterically regulated (AtCM1 and AtCM3) and one cytosolic isoform (AtCM2) that is unregulated. Previous analysis of plant chorismate mutases suggested that the enzymes from early plants (i.e., bryophytes/moss, lycophytes, and basal angiosperms) formed a clade distinct from the isoforms found in flowering plants; however, no biochemical information on these enzymes is available. To understand the evolution of allosteric regulation in plant chorismate mutases, we analyzed a basal lineage of plant enzymes homologous to AtCM1 based on sequence similarity. The chorismate mutases from the moss/bryophyte Physcomitrella patens (PpCM1 and PpCM2), the lycophyte Selaginella moellendorffii (SmCM), and the basal angiosperm Amborella trichopoda (AmtCM1 and AmtCM2) were characterized biochemically. Tryptophan was a positive effector for each of the five enzymes examined. Histidine was a weak positive effector for PpCM1 and AmtCM1. Neither tyrosine nor phenylalanine altered the activity of SmCM; however, tyrosine was a negative regulator of the other four enzymes. Phenylalanine down-regulates both moss enzymes and AmtCM2. The 2.0 A x-ray crystal structure of PpCM1 in complex with the tryptophan identified the allosteric effector site and reveals structural differences between the R- (more active) and T-state (less active) forms of plant chorismate mutases. Molecular insight into the basal plant chorismate mutases guides our understanding of the evolution of allosteric regulation in these enzymes.
Evolution of Allosteric Regulation in Chorismate Mutases from Early Plants.,Kroll K, Holland CK, Starks CM, Jez JM Biochem J. 2017 Sep 28. pii: BCJ20170549. doi: 10.1042/BCJ20170549. PMID:28963347[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kroll K, Holland CK, Starks CM, Jez JM. Evolution of Allosteric Regulation in Chorismate Mutases from Early Plants. Biochem J. 2017 Sep 28. pii: BCJ20170549. doi: 10.1042/BCJ20170549. PMID:28963347 doi:http://dx.doi.org/10.1042/BCJ20170549
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