6eew: Difference between revisions
New page: '''Unreleased structure''' The entry 6eew is ON HOLD Authors: Torrens-Spence, M.P., Chiang, Y., Smith, T., Vicent, M.A., Wang, Y., Weng, J.K. Description: Structural basis for independ... |
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==Crystal structure of Catharanthus roseus tryptophan decarboxylase in complex with L-tryptophan== | |||
<StructureSection load='6eew' size='340' side='right'caption='[[6eew]], [[Resolution|resolution]] 2.05Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6eew]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Catro Catro]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EEW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EEW FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6eei|6eei]], [[6eem|6eem]], [[6eeq|6eeq]]</div></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TDC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4058 CATRO])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aromatic-L-amino-acid_decarboxylase Aromatic-L-amino-acid decarboxylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.28 4.1.1.28] </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=6eew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eew OCA], [https://pdbe.org/6eew PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6eew RCSB], [https://www.ebi.ac.uk/pdbsum/6eew PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6eew ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Radiation of the plant pyridoxal 5'-phosphate (PLP)-dependent aromatic l-amino acid decarboxylase (AAAD) family has yielded an array of paralogous enzymes exhibiting divergent substrate preferences and catalytic mechanisms. Plant AAADs catalyze either the decarboxylation or decarboxylation-dependent oxidative deamination of aromatic l-amino acids to produce aromatic monoamines or aromatic acetaldehydes, respectively. These compounds serve as key precursors for the biosynthesis of several important classes of plant natural products, including indole alkaloids, benzylisoquinoline alkaloids, hydroxycinnamic acid amides, phenylacetaldehyde-derived floral volatiles, and tyrosol derivatives. Here, we present the crystal structures of four functionally distinct plant AAAD paralogs. Through structural and functional analyses, we identify variable structural features of the substrate-binding pocket that underlie the divergent evolution of substrate selectivity toward indole, phenyl, or hydroxyphenyl amino acids in plant AAADs. Moreover, we describe two mechanistic classes of independently arising mutations in AAAD paralogs leading to the convergent evolution of the derived aldehyde synthase activity. Applying knowledge learned from this study, we successfully engineered a shortened benzylisoquinoline alkaloid pathway to produce (S)-norcoclaurine in yeast. This work highlights the pliability of the AAAD fold that allows change of substrate selectivity and access to alternative catalytic mechanisms with only a few mutations. | |||
Structural basis for divergent and convergent evolution of catalytic machineries in plant aromatic amino acid decarboxylase proteins.,Torrens-Spence MP, Chiang YC, Smith T, Vicent MA, Wang Y, Weng JK Proc Natl Acad Sci U S A. 2020 May 5. pii: 1920097117. doi:, 10.1073/pnas.1920097117. PMID:32371491<ref>PMID:32371491</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6eew" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
==See Also== | |||
*[[DOPA decarboxylase|DOPA decarboxylase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aromatic-L-amino-acid decarboxylase]] | |||
[[Category: Catro]] | |||
[[Category: Large Structures]] | |||
[[Category: Chiang, Y]] | [[Category: Chiang, Y]] | ||
[[Category: Smith, T]] | [[Category: Smith, T]] | ||
[[Category: Torrens-Spence, M P]] | |||
[[Category: Vicent, M A]] | |||
[[Category: Wang, Y]] | [[Category: Wang, Y]] | ||
[[Category: Weng, J K]] | |||
[[Category: Aromatic amino acid decarboxylase]] | |||
[[Category: Lyase]] | |||
Latest revision as of 18:24, 8 June 2021
Crystal structure of Catharanthus roseus tryptophan decarboxylase in complex with L-tryptophanCrystal structure of Catharanthus roseus tryptophan decarboxylase in complex with L-tryptophan
Structural highlights
Publication Abstract from PubMedRadiation of the plant pyridoxal 5'-phosphate (PLP)-dependent aromatic l-amino acid decarboxylase (AAAD) family has yielded an array of paralogous enzymes exhibiting divergent substrate preferences and catalytic mechanisms. Plant AAADs catalyze either the decarboxylation or decarboxylation-dependent oxidative deamination of aromatic l-amino acids to produce aromatic monoamines or aromatic acetaldehydes, respectively. These compounds serve as key precursors for the biosynthesis of several important classes of plant natural products, including indole alkaloids, benzylisoquinoline alkaloids, hydroxycinnamic acid amides, phenylacetaldehyde-derived floral volatiles, and tyrosol derivatives. Here, we present the crystal structures of four functionally distinct plant AAAD paralogs. Through structural and functional analyses, we identify variable structural features of the substrate-binding pocket that underlie the divergent evolution of substrate selectivity toward indole, phenyl, or hydroxyphenyl amino acids in plant AAADs. Moreover, we describe two mechanistic classes of independently arising mutations in AAAD paralogs leading to the convergent evolution of the derived aldehyde synthase activity. Applying knowledge learned from this study, we successfully engineered a shortened benzylisoquinoline alkaloid pathway to produce (S)-norcoclaurine in yeast. This work highlights the pliability of the AAAD fold that allows change of substrate selectivity and access to alternative catalytic mechanisms with only a few mutations. Structural basis for divergent and convergent evolution of catalytic machineries in plant aromatic amino acid decarboxylase proteins.,Torrens-Spence MP, Chiang YC, Smith T, Vicent MA, Wang Y, Weng JK Proc Natl Acad Sci U S A. 2020 May 5. pii: 1920097117. doi:, 10.1073/pnas.1920097117. PMID:32371491[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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